australian biochemist 2020 low res.pdfthe asbmb education feature is coordinated by nirma...

VOL 51 NO 1 APRIL 2020 PAGE 1AUSTRALIAN BIOCHEMIST

ISSN 1443-0193

Australian BiochemistThe Magazine of the Australian Society for Biochemistry and Molecular Biology Inc.April 2020, Volume 51, Number 1

VOL 51 NO 1 APRIL 2020AUSTRALIAN BIOCHEMIST

3 Editorial Committee4 From the President7 Publications with Impact

The Black Sheep of the FamilyBalancing the Batteries: the Importance of Coordinated Mitochondrial Protein Synthesis for Energy ProductionPlexin B2: Putting the Trash OutTargeting the Gut Epithelium to Manage ObesityAdvanced Imaging Tips T Cell Target Recognition on its HeadCellular Couriers of Oncogenic Cargo

16 ASBMB Education FeatureImproving Learning Outcomes from Undergraduate Research ExperiencesTeaching Students to Work Effectively in a GroupHarnessing Interdisciplinary Education in Biochemistry and Molecular BiologySo, How Did I Do? Using Student Self-assessment to Steer Feedback

21 SDS PageFrom Undergrad to Postgrad: How to Survive the First Year of Your PhD

22 Competition: Word Search 23 ASBMBMedallistandAwardeeProfiles28 ASBMBFellowshipProfiles30 Science meets Parliament 2019 Report32 Sydney Protein Group: an ASBMB Special Interest Group33 Election of Council 202134 Biochemistry on Stage36 Great Expectations Unexpected Journeys Through Different Research Lands and Scientific Families40 Boomerang Award Report41 Intellectual Property

Artificial Intelligence in Medicine – What is Patentable?43 Science Teachers’ Association of Victoria – Science Talent Search44 Australia Day Honour for ASBMB Member45 In Memoriam49 Our Sustaining Members52 ASBMB Council53 Directory

Table of Contents

Australian Biochemist – Editor Tatiana Soares da Costa, EditorialOfficerLiana Friedman © 2020 Australian Society for Biochemistry and Molecular Biology Inc. All rights reserved.

Front CoverArtist’s rendition of the Golgi apparatus.By Chloe Gleeson.


Australian Biochemist Editorial Committee

Dr Doug FairlieOlivia Newton-John Cancer Research Institute and La Trobe UniversityHeidelberg VIC 3084Email: [email protected] Phone: (03) 9496 9369

EditorialOfficerLiana FriedmanEmail: [email protected]

Associate Professor Tracey KuitSchool of Chemistry and Molecular BioscienceUniversity of WollongongWollongong NSW 2522Email: [email protected]: (02) 4221 4916

Dr Nirma SamarawickremaDepartment of Biochemistry and Molecular BiologyMonash UniversityClayton VIC 3800Email: nirma.samarawickrema@ monash.eduPhone: (03) 9902 0295

Dr Sarah HennebryFPA Patent Attorneys101 Collins StreetMelbourne VIC 3000Email: [email protected]: (03) 9288 1213

EditorDr Tatiana Soares da CostaDepartment of Biochemistry and GeneticsLa Trobe Institute for Molecular ScienceLa Trobe UniversityBundoora VIC 3086Email: [email protected]: (03) 9479 2227

Dr Erinna LeeLa Trobe Institute for Molecular Science and Olivia Newton-John Cancer Research InstituteHeidelberg VIC 3084Email: [email protected]: (03) 9496 9369

Joe KaczmarskiResearch School of ChemistryAustralian National UniversityCanberra ACT 0200Email: [email protected]

Dr Gabrielle Watson Monash Biomedicine Discovery InstituteMonash UniversityClayton VIC 3800 Email: gabrielle.watson@ monash.eduPhone: (03) 9902 9227


It would certainly be fascinating to fast-forward to the end of the year and see where the world lies. Over that time and in the longer term, it will also be interesting to see whether there is any substantial shift in the attitude of both the government and the public towards basic, biomedical and other research. Biochemistry and molecular biology are key disciplines in the race to unlock the secrets of COVID-19 and to generate vaccines and effective treatments. Scientists have probably never had quite such an urgent opportunity to be near the front of people’s consciousness, not to mention the opportunity to be the saviours. I have seen a number of comparisons drawn between this crisis and the issue of climate change, so it will be particularly interesting to see whether this situation has an impact on the climate debate in the longer term.

ConferencesIn this environment, the primary subject of discussion

on the ASBMB Executive and Council has been around the issue of what to do about the ComBio2020 meeting. Conference Chair, Jackie Wilce, and Program Chair, Mark Hulett, together with their organising committee

and the conference organiser, Sally Jay, have been doing a magnificent job over the last couple of years in assembling the program and everything else that is required to organise a major meeting. To make sure that we don’t squander all of that effort, we made the decision to postpone ComBio2020 to 27–30 September 2022. The good news is that we’ve never been so far advanced in our preparations for a ComBio! Several questions arise from this decision:

Is there going to be an ASBMB event this year?At this stage, we are not planning any face-to-face

meetings. However, because one of the main functions of ASBMB is to bring members together for discipline-related discussions, we would like to do something. Currently, we are considering what the best option would be. One option we are exploring is to hold an online symposium dedicated to the question: How have you dealt with the transition to online teaching – what has worked and what hasn’t? Another might be to have something more social, like an ASBMB online trivia event, for example. A third could be to host an online research-focused meeting; I have already seen at least

From the PresidentDear ASBMB Members

This message is to let you know that, due to the COVID-19 pandemic, we have decided to postpone ComBio2020 until 2022. The conference will be held at the Melbourne Convention and Exhibition Centre, with registration starting in late afternoon of Tuesday 27 September, and the full program running from Wednesday 28 September through to Friday 30 September 2022. Thanks to our great organising committee, the program is already very advanced with most of the symposium sessions, chairs and invited speakers in place. See the ComBio2022 website for more information.

Between now and then, we will endeavour to keep our scientificcommunity invigorated with online forums and other communications. We welcome suggestions!

Staysafeandflattenthecurve.

Jackie Wilce (Chair, ComBio2022) and Joel Mackay (President, ASBMB)

Well, the start of 2020 has been quite something. Through Twitter, I have now seen photos of more

of my science colleagues’ pets than ever before, not to mention their spare rooms!

http://www.combio.org.au/combio2022/


a couple of organisations advertise such meetings. This would also give us a chance to showcase the research of our 2020 award winners. Finally, if restrictions on meeting in person ease up towards the end of the year, we might be able to move relatively quickly to host a couple of smaller local meetings that require less organisation (and are consequently cheaper). A meeting of this type might also allow use to showcase the work of the 2020 ASBMB award winners. We welcome any other suggestions.

What is ASBMB now planning for 2021?Our plans for 2021 are to co-host the FAOBMB

Congress in Christchurch in November and to host an extended East Coast Protein Meeting in July. At the moment, we still anticipate that these events will take place and we cross our collective fingers that they will be able to be run successfully.

What about 2023?In our original plans, ComBio2022 was scheduled to

be held in Canberra. However, the Society recently decided to hold an ASBMB-only meeting in odd years. We have resolved to pursue that option for 2023. We are currently in discussions about potential organisers and potential venues for that meeting.

AwardsI’d like to congratulate our 2020 ASBMB award winners:

Professor Trevor Lithgow, Monash University (Lemberg Medal); Professor Colin Jackson, Australian National University (Shimadzu Research Medal); Professor Si Ming Man, Australian National University (Eppendorf Edman ECR Award); Dr Nirma Samarawickrema, Monash University (SDR Scientific Education Award); Dr Matthew Doyle, National Institutes of Health, Bethesda (Boomerang Award); and the ASBMB Fellowship recipients, Dr Amy Baxter, La Trobe Institute for Molecular Science (the Fred Collins Award); Dr Steffi Cheung, University of Melbourne; Dr Mengjie Hu, University of Melbourne; Anukriti Mathur, Australian National University.

The Executive are currently considering the best mechanism to allow our award winners to showcase their work – in lieu of the plan to have them speak at ComBio2020. Stay tuned for more information.

And of course, don’t forget the ASBMB awards for 2021 – think about getting someone to nominate you or encourage a colleague to let you nominate them. We would particularly like female members to consider putting themselves forward – it’s well known that women are less likely to consider themselves for such awards and we would encourage people to think about this and try to help us reverse that long-time trend!

Other mattersOver the last year, Council has developed better

guidelines for our State Representatives and our Special Interest Groups so that we can better serve the membership, and give the State Representatives more voice in shaping the Society. The website has also been updated and refreshed.

In the coming year, I am keen to address several questions:• Should we champion a dedicated Education

symposium?• Should we reactivate an annual Heads of discipline

meeting to discuss shared issues and bring the academic Biochemistry and Molecular Biology community closer together?

• How can we strengthen our contribution to science advocacy?

Please let me know if there are other issues that you think should be considered by the ASBMB.

CouncilFinally, I would like to thank all of the members of the

ASBMB Council for their work for the Society. Briony Forbes as Secretary (being succeeded by Dominic Ng), Marc Kvansakul with his hand on the purse strings, and Jacqui Matthews as President Elect. Tatiana Soares da Costa is doing a great job as our magazine Editor, and is also championing the ASBMB Twitter feed @ITSASBMB, ComBio Twitter feed @ComBio2022 and ComBio on Facebook. Please let her know if you have your own Twitter account so that she can follow it and make sure you follow us too! I would also like to acknowledge the fantastic support we get from Sally and Chris Jay (National Office) and Liana Friedman (Editorial Officer and Webmaster).

I even managed to get though to the end of this piece without mentioning toilet paper – oh, drat!

Joel Mackay President, ASBMB

From the President

https://twitter.com/itsasbmb

https://twitter.com/ComBio2022

https://www.facebook.com/groups/297842333744054/

mailto:T.SoaresdaCosta%40latrobe.edu.au?subject=


02 9575 [email protected]

Dual-independent Auto-cascade compressor system

Castors/ levelling feet

Graphic touch-screen controller

48 hour battery back up

Low-noise 56 db(A)

CFC-free injected insulation

Data-logger/ USB port

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CFC/HCFC-free refrigerant

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480 | 50mm boxesINTRODUCTORYOFFERSpecial price on racks, boxes & tubes.

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Electronic/magnetic door lock

Chart recorder

5x internal doors/shelves

GSM phone alarm

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02 9575 [email protected]

Dual-independent Auto-cascade compressor system

Castors/ levelling feet

Graphic touch-screen controller

48 hour battery back up

Low-noise 56 db(A)

CFC-free injected insulation

Data-logger/ USB port

Key-locked power switch

CFC/HCFC-free refrigerant

320 | 50mm boxes

240 | 50mm boxes

480 | 50mm boxesINTRODUCTORYOFFERSpecial price on racks, boxes & tubes.

MADE IN

EUROPEU LT F R E E Z E R S

OPTIONS

Electronic/magnetic door lock

Chart recorder

5x internal doors/shelves

GSM phone alarm

CO2/LN2 back-up

Underbench models also available

PublicationswithImpactprofilesrecent,highimpactpublicationsbyASBMBmembers. These short summaries showcase some of the latest research by presenting

the work in a brief but accessible manner. If your work has recently been publishedinahighprofilejournal,[email protected].

Publications with Impact

The Black Sheep of the FamilyVuckovic Z#, Gentry PR#, Berizzi AE, Hirata K, Varghese S, Thompson G, van der Westhuizen ET, Burger WAC, Rahmani R, Valant C, Langmead CJ, Lindsley CW, Baell JB, Tobin AB, Sexton PM,

Christopoulos A*, Thal DM*. Crystal structure of the M5 muscarinic acetylcholine receptor.Proc Natl Acad Sci USA 2019;116(51):26001–26007.

#Equal contributors*Correspondingauthors:[email protected],[email protected]

The muscarinic acetylcholine receptors (mAChRs) are a five-membered family (M1–M5) of Class A G protein-coupled receptors (GPCRs) that, together with the nicotinic acetylcholine receptors, mediate the actions of the neurotransmitter acetylcholine throughout the human body. Historically, these receptors are well characterised with the firststudies dating back to the mid 1980s. However, the M5 mAChR has been the black sheep of the family: itwasthelasttobecloned,thelasttobeofficiallyclassifiedasabonafidemAChR in1998and it isthe least studied mAChR. This lack of attention has extended to the determination of its atomic structure, as the structures of the M1–M4 mAChRs have been previously determined. In collaboration with laboratories from Monash University, Vanderbilt University, and the University of Glasgow, the labs of David Thal and Arthur Christopoulos at Monash University were able to determine the M5 mAChR structure, completing the collection of structures for this therapeutically important class of GPCRs.

The mAChRs are involved in a wide range of physiological processes in both the central nervous system (CNS) and the periphery. As such, they have long been valued as drug targets for the design of novel therapeutics. The M1 and M4 subtypes, in particular, have been implicated in Alzheimer’s disease, Parkinson’s disease, schizophrenia and gastrointestinal functions. Although less is known about the M5 mAChR, in part due to the difficulty of designing tool compounds that are selective for each mAChR subtype, knockout M5 mAChR mice exhibit attenuated reward-seeking behaviour to drugs of addiction, such as cocaine and morphine. Furthermore, our collaborators at Vanderbilt University were the first to discover a subtype-selective negative allosteric modulator of the M5 mAChR that, partly through collaboration with our groups, was shown to attenuate ethanol-seeking behaviour and oxycodone self-administration in rats. Collectively, these studies suggest that selective antagonism of the M5 mAChR is a potential treatment for drugs of addiction.

Despite such promising data, further study of the M5 mAChR has been hindered by a lack of small molecular ligands that selectivity target the receptor. The design of such selective ligands has proven challenging, due to the highly conserved acetylcholine orthosteric-binding site combined with a lack of detailed structural information for all five mAChR subtypes. Using lipidic cubic phase crystallography, we were able to determine a high-resolution structure of the M5 mAChR bound to the clinically used antagonist tiotropium. A comparison of all five mAChR subtypes showed a nearly identical orthosteric-binding site. However, comparison of

Comparison of residues lining the extracellular regions of the M2 and M5 mAChR.Residues from the M2 mAChR are shown in dark blue and M5 mAChR in green. Conserved residues are labelled black, and non-conserved residues have coloured labels based on receptor subtype. Chimeric swaps of the ECL regions between the M2 and M5 mAChRs results in a switch in the sensitivity of subtype selective allosteric modulators. Reproduced under a CC BY-NC-ND license.

Y872.61

T/I912.65

Y902.64

E182-1

E/P179-4

Y/R95ECL1

G/D181-2

Y/Q184+1S189+6

N/S4656.58

A/D4696.62

P/K470ECL3 N/V4747.32W4777.35 T/H4787.36

ECL1

ECL2

ECL3

I

II

III

V

VI

VI VIIM2R•NMSM5R•tiotropium

C1830


Balancing the Batteries: the Importance of Coordinated Mitochondrial Protein Synthesis for Energy Production

Rudler DL# , Hughes LA#, Perks KL, Richman TR, Kuznetsova K, Ermer JA,Abudulai LN, Shearwood A-MJ, Viola HM, Hool LC, Siira SJ, Rackham O, Filipovska A*.

Fidelity of translation initiation is required for coordinated respiratory complex assembly.Sci Adv 2019;5(12):eaay2118.

#Equal contributors*Correspondingauthor:[email protected]

The circular mitochondrial genome is a relic of a chance encounter two billion years ago that set the scene for multicellular life. The endosymbiotic union between an ancestral alpha-proteobacterium and a proto-eukaryotic cell created mitochondria, the energy producing organelles within eukaryotic cells. Our second genome, the mitochondrial DNA (mtDNA), encodes a small subset of proteins which are components of the molecular machines that produce energy, known as the oxidative phosphorylation (OXPHOS) system. mtDNA-encoded transcripts and proteins are expressed and synthesised inside the mitochondrial matrix. Mitochondria import all the proteins they require for mtDNA expression and protein synthesis, including nuclear-encoded mitochondrial ribosomal proteins and translation factors that are essential for the production of the mtDNA-encoded proteins. Therefore, both nuclear and mitochondrial gene expression require tight coordination to enable correct assembly and function of the electron transport chain. However, the factors mediating this coordination are not fully understood.

Mitochondrial protein synthesis in animals is unique in that the ribosomes have acquired mitochondria-specific proteins and translate unusual mRNAs which

lack conventional 5′ and 3′ untranslated regions and do not have Shine-Dalgarno sequences found in bacterial mRNAs. Since mitochondrial mRNAs lack these flanking sequences, it is still not clear how mitoribosomes dock and recognise their start codons, suggesting that alternative mechanisms exist that translate leaderless mRNAs. It is likely that mS39 (PTCD3), a mitoribosomal protein we identified and characterised in 2009, interacts with the incoming mRNAs and facilitates their recruitment to the small subunit. However, it was not clear which factors enabled mitoribosomes to initiate translation in the absence of untranslated regions in the mitochondrial mRNAs.

Protein synthesis in mitochondria is overall similar to that of bacteria, beginning with an initiation phase, followed by polypeptide elongation, termination and ribosome recycling. Translation initiation in mitochondria shares similarities with prokaryotic systems, such as the formation of a ternary complex of fMet-tRNAMet, mRNA and the small ribosomal subunit, but differs in the requirements for initiation factors. Bacteria have three initiation factors whose roles are well understood, whereas mitochondria have two initiation factors, MTIF2 that closes the decoding centre and stabilises the binding of the fMet-tRNAMet to the leaderless mRNAs, and MTIF3 whose role was not clear.

Publications with Impactthe extracellular loop (ECL) regions revealed subtle differences that could potentially mediate the selectivity of orthosteric and allosteric ligands. To test this hypothesis, we designed chimeric receptors with ECL regions swapped between the M2 and M5 mAChRs. In pharmacological experiments with the chimeric receptors, we were able to completely switch the sensitivity of an allosteric modulator that is selective for the M2 versus the M5 mAChR, and vice versa. These findings, together with a now completed set of mAChR structures, open the door for future structure-based design of selective drugs.

David ThalMonash Institute of Pharmaceutical Sciences

Monash UniversityFrom left: Wessel Burger, Geoff Thompson,Celine Valant, Emma van der Westhuizen,

David Thal, Ziva Vuckovic and Arthur Christopoulos.



We knocked out the Mtif3 gene in mice to show that this protein is essential for embryo development. Heart- and skeletal muscle-specific loss of MTIF3 caused dilated cardiomyopathy. We identified increased but uncoordinated mitochondrial protein synthesis in mice lacking MTIF3, which resulted in loss of specific respiratory complexes. Our proteomic analyses showed that coordinated assembly of OXPHOS complexes requires stoichiometric levels of nuclearly- and mitochondrially-encoded protein subunits in vivo. Ribosome profiling and transcriptomic analyses revealed that MTIF3 is required for recognition and regulation of translation initiation of mitochondrial mRNAs, but not dissociation of the ribosome subunits. Without the molecular proofreading steps performed by MTIF3, translation initiation proceeds at an accelerated rate but at the expense of fidelity. When fidelity of initiation is compromised, initiation complexes can stall at the 5′ ends of mRNAs, leaving the remainder of the mRNA prone to degradation by 3′–5′ exoribonucleases. Therefore, MTIF3 has a role in proofreading during mitochondrial translation initiation and can destabilise the initiation complex in the absence of mRNA binding to ensure correct assembly of all the components required for protein synthesis.

We established that MTIF3 is essential for coordinated translation initiation and that its loss opens the floodgates of mitochondrial translation but surprisingly

reduces specific respiratory complexes as the ratios of proteins are disturbed; this compromises OXPHOS function and causes dilated cardiomyopathy. Our findings demonstrate that the initiation of mitochondrial protein synthesis fine-tunes the assembly of respiratory complexes, as required for optimal energy production.

Aleksandra FilipovskaHarry Perkins Institute of Medical Research

From left: Oliver Rackham, Laetitia Hughes, Danielle Rudler and Aleksandra Filipovska led the project at the Harry Perkins Institute of Medical Research and Curtin Health Innovation Research Institute, Curtin University.

The mechanism of translation initiation.A. MTIF3 prevents the translation initiation complex formation if it is bound by a tRNA in the absence of mRNA. Only small ribosomal subunits that have bound mRNA before the recruitment of tRNA and MTIF2 are able to proceed from translation initiation to elongation.B. MTIF3 performs molecular proofreading; in its absence, translation initiation proceeds at an accelerated rate but at the expense of fidelity. When fidelity of initiation is compromised, initiation complexes can stall at the start of mRNAs, leaving the remainder of the mRNA prone to degradation.

28S

MTIF3

mRNAtRNAMet

Met

Met

MTIF2GTP

39S

55S

MetMet

GDP

Pre-initiation complex formation

Translation initiation complex

Translation

Met

Met

MetMet

Met

Wild type

MTIF3 knockout

DegradationOverloadedstalling

Protein synthesis

Increased proteinsynthesis

Rate limiting

MTIF3proofreading

MTIF3A B


Every week, we gather our household rubbish in preparation for bin day. Through garbage bags and bins, our waste is stacked in an organised fashion for the swift removal by passing garbage trucks. Similarly, every minute within the human body, our waste consisting of millions of dying cells is being prepared for its efficient removal by the garbagetrucks of the body, i.e. phagocytes. Although the clearance of dead cells is a well-studied concept, howthefinalmomentsofacell’sdeathimpactsitsremoval has been overlooked. For example, it was uncertain if a similar packaging mechanism to our garbage bags occurs and contributes to the rapid removal of dying cells. In our recent study in Cell Reports,weidentifiedanovelroleofthemembranereceptor Plexin B2 in aiding the packaging of dying cellstoassisttheirefficientclearance.

Following the initiation of apoptosis, apoptotic cells can undergo a number of morphological changes, a process called apoptotic cell disassembly, to help the packaging and fragmentation of dying cells. These morphological changes include apoptotic membrane blebbing, thin apoptotic protrusion formation and the generation of large extracellular vesicles called apoptotic bodies. Previously, we identified a new type of membrane protrusion generated by apoptotic monocytes coined beaded apoptopodia that consist of a distinct ‘beads-on-a-string’ structure (Atkin-Smith et al. 2014 Nature Communications). Notably, beaded apoptopodia fragment through a segmentation-like event and release an abundance of apoptotic bodies. To investigate the molecular control underpinning monocyte beaded apoptopodia formation, we performed proteomic analysis on isolated apoptotic bodies from human THP1

monocytes and identified the membrane receptor Plexin B2 to be enriched in apoptotic bodies.

Plexin B2 is best known for its role in aiding cytoskeletal reorganisation such as that occurring in neuronal guidance. However, of the broad Plexin protein family, Plexin B2 is not well characterised and has no previously known functions in cell death processes. Therefore, we examined the role of Plexin B2 during apoptosis and found that Plexin B2 was cleaved by caspase 3 and 7; further, the C-terminal fragment of Plexin B2 was highly enriched in the apoptotic bodies of THP1 monocytes.Excitingly, Plexin B2 now represents a novel caspase 3/7 target and one of the few known markers of monocyte apoptotic bodies.

To determine whether Plexin B2 could also aid the disassembly of apoptotic monocytes, we targeted the expression of Plexin B2 by a CRISPR/Cas9-based approach and monitored the disassembly of Plexin B2-deficient apoptotic cells by time-lapse microscopy. Interestingly, lack of Plexin B2 significantly impaired the formation of beaded apoptopodia and the sequential fragmentation into apoptotic bodies. Furthermore, when incubated with either professional or non-professional phagocytes, lack of Plexin B2 significantly impaired the clearance of apoptotic monocytes. Together, this study identified Plexin B2 as the first positive regulator of monocyte beaded apoptopodia and found it to be required for packaging apoptotic monocytes into apoptotic bodies for the efficient removal by phagocytes.

Georgia Atkin-Smith and Ivan PoonLa Trobe Institute for Molecular Science

La Trobe University

Plexin B2: Putting the Trash OutAtkin-Smith GK, Miles MA, Tixeira R, Lay FT, Duan M, Hawkins CJ, Phan TK,

Paone S, Mathivanan S, Hulett MD, Chen W, Poon IKH*. Plexin B2 is a regulatorof monocyte apoptotic cell disassembly. Cell Rep 2019;29(7):1821–1831.e3.

*Correspondingauthor:[email protected]


Georgia Atkin-Smith and Ivan Poon.

Cartoon of the role of Plexin B2 during monocyte apoptosis and clearance by phagocytes.



The ProblemThe latest Australian Bureau of Statistics National

Health Survey (2018) revealed that two thirds of Australian adults and one quarter of children aged 5–17 were overweight or obese. Obesity is strongly linked to the development of multiple comorbidities including cardiovascular disease, high blood pressure, Type 2 diabetes (T2D), insulin resistance (IR) and metabolic syndrome (1–3), which has a major impact on Australia’s economy. It is estimated that the combined (indirect and direct) annual cost of treating obesity-related comorbidities is now approaching AUD $10 billion (4). While lifestyle changes such as diet and exercise are clearly effective in reducing and preventing obesity, these are often difficult to maintain. New approaches for preventing and managing obesity are therefore clearly needed.

A New DiscoveryOur group recently discovered that ablation of the

histone deacetylase 3 (HDAC3) protein, specifically in the intestinal epithelium, protects mice against diet-induced obesity (5). Investigation of the mechanisms driving this effect revealed that deletion of the Hdac3 gene induced an increase in expression of lipid oxidation genes in intestinal epithelial cells, which was due to ‘de-

repression’ of the PPAR family of transcription factors, particularly PPARa. The increased levels of lipid oxidation genes were associated with an increased rate of lipid oxidation and, in turn, reduced levels of cellular lipids in the intestinal epithelium of Hdac3 knockout mice. Importantly, this translated into lower levels of circulating triglycerides, which we propose manifests in the leaner phenotype of these mice over time. We were subsequently able to demonstrate that the gene expression changes induced by Hdac3 deletion could be reproduced, at least in part, using a small molecule inhibitor of HDAC3 activity (RGFP966), unveiling a potential new pharmacological strategy for managing obesity.

A Glimpse into the FutureThese findings establish a central role for HDAC3

in coordinating PPAR-regulated expression of lipid oxidation genes in the intestinal epithelium and consequently the rate of lipid metabolism in this tissue, thus identifying intestinal HDAC3 as a potential therapeutic target for preventing obesity and related diseases. Essential to this will be the development of innovative drug delivery strategies, which enable HDAC3 inhibitors to be locally delivered and retained in the intestinal epithelium.

Targeting the Gut Epithelium to Manage ObesityDávalos-Salas M, Montgomery MK, Reehorst CM, Nightingale R, Ng I, Anderton H, Al-Obaidi S, Lesmana A, Scott CM, Ioannidis P, Kalra H, Keerthikumar S, Tögel L, Rigopoulos A, Gong SJ,

WilliamsDS,YoganantharajaP,Bell-AndersonK,MathivananS,GibertY,HiebertS,Scott AM, Watt MJ*, Mariadason JM*. Deletion of intestinal Hdac3 remodels the lipidome

of enterocytes and protects mice from diet-induced obesity. Nat Commun 2019;10(1):5291.*Correspondingauthors:[email protected],[email protected]

Proposed model of fatty acid metabolism in intestinal epithelial cells in (A) Hdac3WT and (B) Hdac3IKO mice. Dietary lipids (blue) enter intestinal epithelial cells via the apical membrane. Within the cell, fatty acids undergo multiple fates including (1) metabolism via b-oxidation in the mitochondria and peroxisomes, and (2) packaging into chylomicrons (ChM, yellow circles) for shipment to peripheral organs. In wild-type mice (A), expression of b-oxidation genes are repressed by HDAC3, and the rate of b-oxidation is low. Consequently, the majority of fatty acids are packaged into ChM for export. Comparatively, the loss of HDAC3 (B) results in constitutive expression of b-oxidation genes and increased rate of fatty acid oxidation. This in turn leads to lower levels of fatty acids being available for packaging into ChM and export.


References1. Cani PD, Delzenne NM, Amar J, Burcelin R (2008)

Pathol Biol 56(5):305–309.2. Canfora EE, Meex RCR, Venema K, Blaak EE

(2019) Nat Rev Endocrinol 15(5):261–273.3. Reviewed in https://www.who.int/en/news-room/

fact-sheets/detail/obesity-and-overweight4. Reviewed in PwC report: Weighing the cost of

obesity: a case for action, 2015.5. Dávalos-Salas M, et al. (2019) Nat Commun

10(1):5291.Mercedes Dávalos-Salas and John Mariadason

Olivia Newton-John Cancer Research Institute and La Trobe University School of Cancer Medicine


Members of John Mariadason’s group.

T cells represent a key component of our immune system and play a critical role in protecting us against harmful pathogens, like viruses and bacteria, and cancers. The more we understand how they recognise, interact with and even kill infected or cancer cells, the closer we move to developing therapies and treatments for a range of conditions. The research groups of Jamie Rossjohn(BiomedicineDiscoveryInstitute,MonashUniversity) and Dale Godfrey (Peter Doherty Institute, University of Melbourne) reported the MHC-I like molecule, MR1, as a ligand for human gd T cells

and determined the crystal structure of a gd T cell receptor (TCR) in complex with the MR1 molecule, whichcompletelyredefinedtheparametersofTCRrecognition determinants.

During the course of evolution, the immune system of vertebrates has consistently and remarkably adapted to protect itself from pathogens such as bacteria, yeast, viruses and parasites, to enable reproduction and ensuring the survival of the species. To achieve this, the immune system of vertebrates comprises a complex network of cells, organs, tissues, proteins and molecules that collectively constitutes the primary line of defence against various pathogens. In particular, T cells represent a key component of our immune system. They express cell surface receptors called TCRs. TCRs have the ability to recognise pathogen-derived molecules termed antigens (Ags). These encompass proteins, lipids, metabolites and carbohydrates, which are presented to the major histocompatibility complex (MHC). In collaboration with the Godfrey laboratory, our research is primarily focussed on understanding the mechanism that underpins this recognition event at the cellular and molecular level. T cells can be divided into two main groups based on the genes that encode their TCRs, namely ab and gd T cells. Over the last decades, studies in T cell-mediated immunity have focused on understanding the presentation of peptide-derived Ags by the MHC, and their molecular recognition by ab

Advanced Imaging Tips T CellTarget Recognition on its Head

Le Nours J#, Gherardin NA#, Ramarathinam SH, Awad W, Wiede F, Gully BS, Khandokar Y, Praveena T, Wubben JM, Sandow JJ, Webb AI, von Borstel A, Rice MT, Redmond SJ,

Seneviratna R, Sandoval-Romero ML, Li S, Souter MNT, Eckle SBG, Corbett AJ, Reid HH, Liu L, Fairlie DP, Giles EM, Westall GP, Tothill RW, Davey MS, Berry R, Tiganis T, McCluskey J, Pellicci DG,PurcellAW,UldrichAP,GodfreyDI*,RossjohnJ*.Aclassofgd T cell receptors recognizethe underside of the antigen-presenting molecule MR1. Science 2019;366(6472):1522–1527.

#Equal contributors*Correspondingauthors:[email protected],[email protected]

Members of the Biomedicine Discovery Institute,Monash University, involved in the study, from left:Jérôme Le Nours, Benjamin Gully and Wael Awad.



A. Crystal structure of the G7 gdTCR-MR1-5-OP-RU ternary complex.

B. Small angle X-ray scattering (SAXS) of the ternary complex.

TCRs. However, ab and gd T cells can respond to other classes of Ags associated with both protective and aberrant immunity; our understanding of non-peptide-centric ab and gd T cell mediated immunity in humans is still poorly understood. In this recent study, we have identified a novel target molecule for gd T cells, known as the MHC-related 1 molecule (MR1). MR1 shares structural similarities with the classical MHC molecules, although it has evolved to accommodate a chemically distinct class of Ags, namely microbial vitamin B-derived metabolites. This first major discovery suggests that gd T cells may play a role in infection via this pathway, and reveals MR1 as a potential novel target for manipulating this poorly characterised class of T cells. Further, using X-ray crystallography, we determined the structure of the first ternary complex of a human gd TCR bound to MR1. Our structural studies led to a very intriguing result whereby the gd TCR was bound underneath the MR1-Ag binding groove for recognition, contrasting with the prevailing view that T cell receptors invariably sat atop the MHC and MHC-like molecules for recognition. This discovery has redefined what we thought we knew about T cell recognition for the past 20 years and represents a major advance in the field of T cell biology. The gd T cells represent an important population in various types of immunity, including tumor and microbial immunity. These new insights will have major implications for our understanding of gd T cell biology and should ultimately give rise to new approaches to target this broader family of cells in both infectious and non-infectious diseases.

Jérôme Le NoursBiomedicine Discovery Institute

Department of Biochemistry and Molecular BiologyMonash University

β-catenin is a highly conserved multifunctionalprotein that has been implicated in canonical Wnt signalling pathway and cell adhesion. Wnt signalling is an evolutionarily conserved pathway that plays a fundamental role during embryonic development and tissue homeostasis. However, aberrant Wnt signalling resulting from mutations ofkeygenesincludingAPCandβ-catenincanleadto a wide variety of human diseases. It has been known for some time that approximately 93% of all colorectal cancer (CRC) have mutations in at least one gene implicated in the Wnt signalling pathway.

Amongthese,mutationsinβ-catenin,especiallyinthe phosphorylation sites that regulate the stability (S33, S37, T41, S45), can lead to the constitutive activation of Wnt signalling pathway thereby resulting in increased cell proliferation.

Extracellular vesicles (EVs) are considered mediators of intercellular communication both at local and distant sites. EVs mediate cell-to-cell communication through the horizontal transfer of cargo molecules including proteins and nucleic acids. It is now well established that EVs regulate various pathophysiological processes in favour of cancer progression, including remodelling

Cellular Couriers of Oncogenic CargoKalra H, Gangoda L, Fonseka P, Chitti SV, Liem M, Keerthikumar S, Samuel M,

BoukourisS,AlSaffarH,CollinsC,AddaCG,AngCS,MathivananS*.Extracellularvesiclescontainingoncogenicmutantβ-cateninactivateWnt

signalling pathway in the recipient cells. J Extracell Vesicles 2019;8:1690217.*Correspondingauthor:[email protected]



Extracellular vesicles can mediate the intercellular transfer of oncogenic cargo including mutant β-catenin and aid in the increase of Wnt signalling, proliferation, migration and tumour burden.

the tumour microenvironment, immune evasion, coagulation, vascular leakiness, establishing pre-metastatic niche, tropism for metastasis, transfer of chemoresistance and metastasis. In this study, we examined whether the oncogenic mutant β-catenin, that is constitutively active, can be transferred to neighbouring cells and be functional. To understand if mutated β-catenin can be secreted via EVs, an integrative proteogenomic analysis was performed using exome sequencing data of LIM1215 human CRC cells and proteomics data of EVs isolated. The analysis confirmed the presence of high amounts of mutant β-catenin in EVs. Follow-up analysis confirmed that EVs carrying mutant β-catenin altered the Wnt signalling activity in RKO CRC cells that bear wild-type β-catenin, both in vitro and in vivo. SILAC-based quantitative proteomics analysis confirmed the intercellular transfer of mutant β-catenin via EVs to the nucleus of the RKO cells. In addition to Wnt signaling activity, incubation of EVs with the recipient cells increased the migration of RKO cells. Intravenous administration of β-catenin containing EVs activated the Wnt signalling pathway and increased the tumour burden of mice implanted with RKO cells. Although the increase in migration of RKO cells or the tumour burden upon treating with EVs should be formally attributed to the entire EV cargo and not to mutant β-catenin alone, this study emphasises that EVs could switch the phenotype of the neighbouring and distant cells in favour of cancer progression.

It is well known that tumours are comprised of different subpopulations of cancer cells that exhibit salient

genetic and behavioral variations leading to intratumour heterogeneity. Therefore, different clonal subpopulations bearing different mutational loads could potentially interact with each other and with normal and stromal cells via EVs. Hence, several groups around the world envision the targeting of cancer cell EV secretion as a viable strategy to reduce tumour burden and metastasis. The results from this study suggest that circulating EVs can be rapidly taken up by the target cells in the tumour microenvironment and allows for the amplification of the signal in favor of tumour progression.

Lahiru Gangoda and Suresh MathivananLa Trobe Institute for Molecular Science

La Trobe University

Mathivanan group from La Trobe University.


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ASBMB Education FeatureThe ASBMB Education Feature is coordinated by Nirma Samarawickrema

([email protected])andTraceyKuit([email protected]).

Undergraduate research experiences (UREs) are generally agreed to be a good idea as they provide students with an introduction to authentic research. While they are usually a positive experience, the learning outcomes students achieve are more problematic. We investigated this with an OLT-funded project nearly ten years ago. Since then, we have analysed data from more than 300 students to understand what students actually learn and how they perceive their supervision.

One thing we noticed was a mismatch between learning outcomes expected by supervisors and what students reported they learnt. Fig. 1 shows a hierarchical description of potential learning outcomes; most supervisors want their students to obtain the full range. However, students’ reported learning gains are generally confined to the less complex outcomes in the lower two tiers. To address this mismatch, we have suggested three tips for good URE supervision. More extensive analysis is published elsewhere (1–3).

1. Focus on learning, rather than research outcomes. Research is all about successful outcomes and we (often unconsciously) convey this to our students. In addition, when UREs are assessed through a lab report, which also emphasises results, students may equate getting results with a good project. However, we observed that the more complex learning outcomes were often evident when projects didn’t go well, as students then became more engaged with the process of research. Troubleshooting is an essential part of research but students might not understand this and sometimes interpret failure to get results as a personal failing. The supervisor has a critical role in normalising failure by discussing their own experiences and the importance of problem-solving skills. Students value a supportive supervisor who helps them develop alternative approaches without putting them under pressure to achieve positive results.

2. Test your assumptions about what a student knows. Students may not have the background knowledge to understand the scope or detail of your research project. Ask them about what relevant courses they have taken and listen to their answers.

Students need to feel that it is OK to admit to ignorance and ask ‘silly’ questions. We saw many occasions where misunderstandings between students and supervisors arose because everyone assumed they knew what they were doing.

3. Designtheprojectcarefully.A good project is one with a clear and achievable goal within the limited time available in most UREs. Although much research today is done by multidisciplinary teams, your student should have some goals for their own small part. Students who just slotted into someone else’s project generally reported a poor experience. Students value feeling ownership of their project and that they are trusted to make a contribution to your research, so make their role clear.

These three things might seem obvious but we know from our extensive student data that they are often overlooked. Supervision is the single most important factor in determining the student experience (1,4). You can support more complex learning by your student by helping them reflect on the scientific thinking behind the project as well as its day to day operation.

Improving Learning Outcomes fromUndergraduate Research Experiences

Susan Howitt, Research School of Biology,Australian National University

Fig 1. Potential learning outcomes from undergraduate research experiences.

mailto:nirma.samarawickrema%40monash.edu?subject=


ASBMB Education Feature

Teaching Students to Work Effectively in a GroupNirmani Wijenayake, School of Biotechnology

and Biomolecular Sciences, UNSW Sydney

The potential learning benefits of group work are manifold. However, students are seldom taught how to work effectively in a group. Consequently, some students dislike group work and consider it stressful. The practical component of a second year Fundamentals of Biochemistry course at UNSW is assessed in part through a group project. The task involves designing an experimental protocol and applying it to identify a metabolic disorder discussed in class. To encourage students to work effectively in groups, we undertook the following:• Randomly allocating students into groups of four

to promote diversity (course of study, cultural background, prior experience).

• Supporting students to connect by providing icebreaker exercises. For example, to explore each other’s comfort with public speaking, students asked one another: Would you rather give or write the presidential speech?

• Challenging students with a fun, low stake task to strengthen connections (e.g. build the tallest structure possible to support a marshmallow using 40 spaghetti sticks, scissors and cello tape – Fig. 1). Students had to brainstorm together to address this challenge.

• Providing opportunities for conflict resolution within groups. Students were provided scenarios involving group work, which they had to appraise as a group to identify the issue, discuss strategies of resolution and develop a set of ground rules which they agreed to abide by.

• Encouraging reflection by maintaining a weekly diary about their group experiences and thoughts about group work, which was monitored by staff. These reflections enabled staff to better understand issues experienced, and identify strategies of support and interventions needed. As this task was assessed, students were provided with prompts to facilitate reflection, for example: What is your general attitude

towards group work? How do you demonstrate trust and openness towards others in your group?

• Establishing group-based assessments through a quiz, which the students completed individually and later finalised as a group. Working through the quiz as a group enabled consolidation of knowledge through peer-teaching/learning.

• Teaching students to benchmark their work by peer-assessing draft reports, such that students develop a dialogue between their work, others’ work and standards. This enabled students to recognise that there are multiple approaches to diagnose a metabolic disease and helped them learn from each other.

• Supporting students to communicate their findings through group oral presentations.

Overall, students did extremely well in the assessment, with a mean score of 88%. Using a Likert scale survey, we explored student perspectives of group work. The majority (88%) of students agreed or strongly agreed

Fig. 1. Building a structure to support a marshmallow.

References1. Howitt SM, Wilson AN, Wilson KF, Roberts P (2010)

High Educ Res Dev 29(4):405–420.2. Wilson A, Howitt S, Higgins D (2016) Assess Eval

High Educ 41:901–916. 3. Wilson A, Howitt S, Higgins D (2016) Assess Eval

High Educ 41:885–901.4. Russell SH, Hancock MP, McCullough J (2007)

Science 316(5824):548–549.

Professor Susan Howittis Head of the Biology

Teaching and Learning Centre,Australian National University.

[email protected]


Fig. 2. Student perception of group work(5 = strongly agree, 1 = strongly disagree).

ASBMB Education Featurethat through the group activity they learned invaluable skills (Fig. 2) such as: • Strategies to meet deadlines• Problem solving through open discussions• Understanding some aspects of scientific research • Having the flexibility to be creative • Improving presentation skills• Seeing the real-life applications of biochemistry• Sharing the workload• Using feedback to improve their work• Learning through teaching

Many students commented that the assessment task helped them to ‘make new friends’, ‘trust and rely on each other’ and ‘work effectively as a group’. As the semester progressed, students built a good rapport with members of their groups. Staff felt that this was reflected by better engagement with group work.

Dr Nirmani Wijenayake is an Education-focused Lecturer

and the Acting Deputy Director of Teaching in the School of

Biotechnology and Biomolecular Sciences, UNSW Sydney.

[email protected]

The Education conference, Harnessing Interdisciplinary Education in Biochemistry and Molecular Biology, was run by the International Union of Biochemists and Molecular Biologists (IUBMB) and the Philippine Society for Biochemistry and Molecular Biology (PSBMB) on 13–15 November 2019 in Manila, the Philippines. The conference included keynote and plenary presentations and parallel sessions. The parallel sessions consisted of short talks followed by round table discussions to give attendees the opportunity to have in depth discussions with the presenters and other attendees. Jessica Gibbons, Monash University, won the Best Education Poster Award.

Biochemistry and molecular biology are studied by students in programs ranging from science to health sciences, medicine and agriculture. As many of us know, when teaching in these varied programs, we can face a range of challenges as well as those issues specific to teaching students at various levels from K–12 through to postgraduate. Hence the conference was themed around program disciplines and levels and also included continuing education in industry. Talks and discussions covered many interesting topics and the

broad international representation (attendees came from 22 countries) gave insights into the varied challenges facing educators around the world. There were over 400 attendees at the conference, including 20 winners of IUBMB Tang Travel Bursaries.

Harnessing Interdisciplinary Educationin Biochemistry and Molecular Biology –

an IUBMB Education ConferenceJanet Macaulay, Monash Biomedicine Discovery Institute,

Monash University

Fig. 1. Conference co-chairs Gracia Fe Yu (left; Chair of FAOBMB Education Committee, University of the Philippines) and Janet Macaulay.



Professor Janet Macaulay is Chair of the Committee

for Education and Training, IUBMB, and Associate

Editor of Biochemistry and Molecular Biology Education.

[email protected]

Fig. 2. Panel discussion speakers, from left: Philip Poronnik (University of Sydney), Xiaoyun Lu (Xi’an Jiaotong University, China), Anat Yarden (Weizmann Institute of Science, Israel) and Joseph Provost (University of San Diego, USA).

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Researching and sharing our knowledge and understanding of education should be a core component of what we do as educators. The IUBMB journal, Biochemistry and Molecular Biology Education (BAMBEd), which aims ‘to enhance teacher preparation and student learning in Biochemistry, Molecular Biology and related sciences’ such as Biophysics and Cell Biology, facilitates the worldwide dissemination of educational material and scholarship. Hence, one of the conference parallel sessions was ‘Publishing in Education’ and included Phillip Ortiz, Editor in Chief of BAMBEd. All conference speakers were invited to contribute to a BAMBEd special issue, based on conference presentations, which will be published in 2020.

As well as gaining much from our wonderful discussions on education, we enjoyed the beautiful historic Manila Hotel conference venue and the excellent organisation and hospitality of our Filipino hosts. The conference dinner included wonderful food and a fascinating display of traditional culture and dance.

The IUBMB is committed to supporting education and training in a number of ways, including through an ongoing program of collaborative biannual education conferences in varied geographical regions. This was the second conference; the first was held in 2017 at the Weizmann Institute of Science, Israel. Plans are in progress for the 2021 conference, which will be run in conjunction with the American ASBMB. The proposed topic is ‘Big Data Science to Unify Teaching and Research’. Details of other opportunities are available on the IUBMB website and include funding for educational activities and education and research fellowships. You can also join the Friends of IUBMB to hear what’s going on.

https://iubmb.onlinelibrary.wiley.com/journal/15393429

https://iubmb.org/friends-of-iubmb/



It is well recognised that effective feedback is crucial for motivating students to improve their work. Students need to participate actively in this process, alongside their educators, in order to maximise the relevance of feedback to the students themselves. However, to achieve this, students first need to be able to accurately assess the quality of their own work, identify and articulate areas they find challenging. This would facilitate a shift from the more passive model of feedback as information transfer from educator to student, to one that creates a dialogue between educator and student (Fig. 1). We sought to determine whether providing students with a structured self-assessment template prior to submission of reports influenced their confidence in assessing their own work and modulated their perceptions of subsequent feedback.

We devised a check sheet for students to complete prior to submitting their laboratory reports. Each check sheet was incorporated into the laboratory report template and included key learning outcomes that students were expected to have achieved upon completing the class activity. We queried students on their performance against each learning outcome, aspects they did well and

those that they found challenging. Teaching Associates (TAs) marked each student’s practical report on content, assessed student performance relative to the learning outcomes and focussed on areas of difficulty identified by the students. Thus, students received feedback on their report and on the accuracy of their self-assessment.

In response to an end-of-semester survey, the majority of students indicated that they completed the check sheet honestly and accurately. Approximately half of the students indicated that their self-assessment matched that of their TA to some extent, with a similar proportion finding subsequent feedback for their report useful. The most frequently chosen reason for finding this feedback useful was that students could first nominate what they found challenging. This suggests that students are willing to reflect on their work, if given the opportunity.

It is also possible that for students whose self-assessment did not match those of their TA’s, this could negatively influence how they responded to feedback. Although students need guidance in calibrating their ability to self-assess accurately, this skill needs to be developed in a supportive and sensitive manner. Students should also be given opportunities to demonstrate learning from feedback provided in future tasks.

Despite this exposure to a structured form of self-assessment, nearly half the student cohort indicated that they still lacked confidence in doing this. It is therefore unsurprising that they were equally divided as to whether they were likely to change the way they approached self-assessment in the future.

We have trialled this initiative with two separate student cohorts (Pharmacology and Biochemistry) at similar points in their degrees. Both cohorts share an overall lack of confidence assessing the standard of their work. This highlights the need to embed more opportunities for students to practice self-assessment early in their university life, in order to gain confidence and recognise its importance. Only then can we realistically expect students to gain the most from feedback that will be valuable and relevant to them.

So, How Did I Do?Using Student Self-assessment to Steer Feedback

Klaudia Budzyn, Department of Pharmacology, Monash University

Dr Klaudia Budzyn is anEducation-focussed Lecturer

in the Departmentof Pharmacology,

Monash [email protected]

Fig. 1. The current model of feedback (top) relies on one-way transmission of information. However, the model where students have input into feedback sets up a cycle of student reflection and evaluation that will inform feedback (bottom), which can then be used by students to further reflect, evaluate and develop strategies for improving future tasks. Ultimately, this closes the feedback loop.


The start of your PhD can be an exciting yet daunting experience. Throughout your Bachelors study, and perhaps even a Masters program, your studies and research are closely guided by academics, including your supervisor. Therefore, the transition to undertaking PhD work can come as a shock to many, perhaps even leading you to ask: Did I make the right decision to do my PhD?; Can I really handle the pressure of a PhD?; Will three years be enough time to finish my project? It is easy to forget you’re not alone in this experience and that it is impossible to predict everything from day one. However, there are ways to make the most of the transition into your PhD program and to navigate the pitfalls commonly encountered in your first year.

1. Look after yourselfA PhD program is hard, and I have yet to meet anyone

that would say otherwise. The stress and self-imposed long hours can take a massive toll on your health, and not just physically. The prevalent self-doubt and anxiety will be mentally draining. The frequent failures in the laboratory will make you question your decision to ever start a PhD in the first place. So, from day one, make sure to find a healthy work–life balance and don’t succumb to the common mistake of letting your PhD work consume your life. Whether it be spending time with friends and family, going to the gym or even picking up a hobby at home, finding a way to switch off when you leave the lab for the day will help you find this balance. But, if you do start to feel crushed by the pressure, no one will judge you for taking a break and looking after yourself. You have three years ahead of you, so you don’t need to do all your experiments in one month.

2.Don’t be afraid of your supervisor, they won’t biteAlthough we often forget, each of our supervisors has

been in our shoes before. They will have completed their own PhDs well before us and they all understand how the start of a PhD program can be overwhelming. Don’t be afraid to communicate with your supervisor about the struggles you are facing, both in and out of the lab. They are there to help guide you through your PhD studies, so the more open and honest you are with your supervisor, the more they can help you succeed.

3. Apply for grants, no matter how smallWhilst the Australian PhD stipend is more generous

than in most countries, it is still a far cry from the money

you would earn at a full-time job. However, there are numerous grants out there designed to ‘top-up’ your current scholarship or cover travel costs associated with attending conferences. Even if you don’t think you stand a chance, apply for the grants because if you don’t try, you will never know. Not only will these grants help you financially, but receiving funding during your PhD studies will look good on your CV when it comes time to apply for postdoctoral positions.

4. Read, read, readI won’t be the first person to tell you to read widely and

deeply, and I definitely won’t be the last. Reading papers and keeping up with the current literature in your field will be one of the most beneficial things you can do throughout your PhD program. While you are still figuring out your project, spend some time catching up on the literature in your field. It will assist you with your research planning and experimental design, at the same time opening your mind to new ideas and technologies that can make your project stand out. And once your project eventually gets started, keep reading because new papers are published all of the time and you never know what you’ll learn.

5.Lastbutnotleast,enjoyyourPhD!Your PhD program is going to be a huge part of your life

for the next few years. It will be tough and there will be times when you wish you had chosen a ‘normal’ career, but don’t forget that your PhD will be a life-changing experience. By the end of the three or so years of research, writing, giving talks and attending conferences, the highs will far outweigh the lows. These activities also provide essential skills development along your doctoral journey. So, celebrate the successes and learn from the failed experiments. Most importantly, have fun and enjoy the moment whenever you can.

Jessica Wyllie is a PhDcandidate at the La Trobe

Institute for Molecular Science. [email protected]

SDS Page: Short Discussions for Students Page

From Undergrad to Postgrad:How to Survive the First Year of your PhDJessica Wyllie, La Trobe Institute for Molecular Science


Presenting the latest competition for the members of ASBMB. All correctentries received by the Editor ([email protected]) before May 2020

will enter the draw to receive a gift voucher. With thanks to Joe Kaczmarski.

Complete the word search below.The unused letters along the shaded diagonal can be

unscrambled to spell the name of a common type of molecule.

Competition: Word Search

ASBMB BIOCHEMISTRY CATALYSIS CELLCRISPR DNA ENZYME EVOLUTIONGENE GLUTATHIONE GLYCOPEPTIDE KISTAMICINLIPID METABOLISM NMR PCRPHAGE PROTEASOME RESEARCH RIBOSWITCHSYNBIO VESICLE VIRUS

Presenting the latest competition for the members of the ASBMB. All correct entries received by the Editors ([email protected]) before XXXXXX will enter the draw to receive a gift voucher. With

thanks to Joe Kaczmarski.

COMPETITION: Word Search

Complete the word search below. The unused letters along the shaded diagonal can be unscrambled to spell the name of a common type of molecule.

ASBMB BIOCHEMISTRY CATALYSIS CELL CRISPR DNA ENZYME EVOLUTION GENE GLUTATHIONE GLYCOPEPTIDE KISTAMICIN LIPID METABOLISM NMR PCR PHAGE PROTEASOME RESEARCH RIBOSWITCH SYNBIO VESICLE VIRUS

R E N H A G O P W H N C R I S P R O

A D D T Z O G V I R U S X Z P S M B

M R Y I E A G W K T X P R X G D E Y

D P R O T E A S O M E N M R Y Y T S

N X S D N P V A S B M B Y I X R A W

A U G E M R E Y E L C I S E V T B G

P J S P T O N P I F S R R T S S O Z

E V L R W B O T O U A E I R I I L A

N V T I I K B Q O C S K I P S M I S

O C O O P E I W N E Y B O T Y E S H

I F T L E I R S A L O L O Z L H M M

H H M H U Q D R T S J B G Y A C T C

T I Q V J T C I W A N D E Q T O E E

A Q E M H H I I Q T M A J A A I W L

T F Q G Z K T O W J P I Z E C B A L

U W Z Y A C Z E N N X P C R M C F E

L A E H H H Y B E X H U C I C C A W

G F T G V D P E N Z Y M E F N M J H

UNSCRAMBLED ANSWER: _____________________________


ASBMB Medallist and Awardee Profiles

The Lemberg Medal is awarded to a distinguished Australian biochemist or molecular biologist who will present the Lemberg Lecture at the annual ASBMB conference. The Medal is presented in memory of Emeritus Professor MR Lemberg, who was the Society’s first President and Honorary Member. Nominees must have been members of the Society for at least five years before the year in which the Medal nomination is to be considered. An honorarium is provided by ASBMB.

The Lemberg MedalTrevor Lithgow

Professor Trevor Lithgow graduated with a PhD in Biochemistry from La Trobe University in 1992. In 1993, he was awarded a Long-Term Fellowship from the Human Frontiers Science Program and moved to a postdoctoral position with Professor Gottfried (Jeff) Schatz at the University of Basel. In an unforgettable time in Switzerland; he worked to identify the components of the TOM complex, the key factor required in mitochondria for protein import and thereby organelle biogenesis. Ten papers were published on the discovery of the protein import receptors Tom20/Mas19 and Tom22/Mas22, including a paper in Nature reconstituting the initial steps of protein import and a review in Trends in Biochemical Sciences that set the model for how receptor cooperativity delivers protein substrates to the TOM complex, a fascinating molecular machine. In 1999, Lithgow was awarded the HFSP Tenth Anniversary Award that recognised the top ten Research Fellows in the first ten years of the Human Frontiers Science Program. A capstone to these discoveries came with recent work on the high-resolution structural analysis of the TOM complex published in three papers in Science, Molecular Cell and Nature.

In 1996, Lithgow was recruited to La Trobe University to start his own laboratory, and in 1999 the lab moved to the Department of Biochemistry and Molecular Biology, University of Melbourne. In teaching, he developed three new subjects in Molecular Biology: a third year Molecular Aspects of Cell Biology unit, a multidisciplinary second year subject Integrated Biomedical Sciences I, and the Department’s first molecular cloning practical subject that used PCR, cDNA library screening and bioinformatic analysis to train approximately 150 students per year in these core techniques and the concepts for which they provide evidence.

In 2008, Lithgow was awarded an ARC Federation Fellowship to build capacity for studying host–pathogen interactions at Monash University. In 2014, he took up an ARC Laureate Fellowship to develop nanoscale imaging approaches to investigate bacterial cell biology. This included developing applications of single particle cryoEM, neutron reflectrometry, atomic force microscopy and super-resolution imaging of bacterial cells. The fundamental discoveries from this work include how bacterial outer membranes are assembled and the intracellular complexity of the bacterial cytoplasm and periplasm. Lithgow also led the NHMRC Program in Cellular Microbiology that used the fundamental knowledge of bacterial cell biology to better understand mechanisms of antibiotic resistance, the mechanics driving entry of bacteriophage into bacteria and the mechanisms by which phages control host cell biology. In 2010, he was elected as a Fellow of the Australian Academy of Science.

In 2020, Professor Lithgow was appointed as Director of the Centre to Impact AMR, in order to find sustainable solutions to the growing and global problem of antimicrobial resistance.

The ASBMB Award recipients were to receive their awards, and the Lemberg Medal, Shimadzu Research Medal, SDR Scientific Education Award, Eppendorf Edman ECR Award and Boomerang Award recipients would have delivered their presentations at ComBio2020, which has now been cancelled due to the COVID-19 pandemic. Arrangements for the presentation of awards and delivery of the relevant lectures will be announced in due course. Many of the awards contain a travel component and each awardee had specified a conference or other training activity to which their award was to be applied. Since international travel and conference activities have largely been suspended, alternative arrangements will be made for these recipients to utilise their awards at a later date.


ASBMB Medallist and Awardee ProfilesThe Shimadzu Research Medal is awarded to an outstanding Australian biochemist or molecular biologist with less than 15 years postdoctoral experience. The successful candidate will present the Shimadzu Medal Lecture at the ASBMB annual conference. Nominees must have been members of the Society for at least two years before the year in which the Medal nomination is to be considered. An honorarium is provided through the courtesy of Shimadzu.

The Shimadzu Research MedalColin Jackson

Professor Colin Jackson heads the Chemical and Structural Biology Laboratory at the Research School of Chemistry (RSC), Australian National University. He is also the Associate Director of Research of the RSC.

Colin’s graduate studies with Professor David Ollis defined the mechanistic basis for phosphate ester hydrolysis in a number of enzymes and was the beginning of an interest in the link between protein structural dynamics and function (Proceedings of the National Academy of Sciences USA, 2009). His PhD was awarded in 2007. He subsequently accepted a team leader position at the CSIRO after a short postdoctoral fellowship, where he worked with Dr John Oakeshott on the evolution of enzymes involved in insecticide resistance (Proceedings of the National Academy of Sciences USA, 2013). After being awarded a Marie Curie Fellowship, Colin then trained with Professor Martin Weik, an expert in kinetic crystallography, at the Institut de Biologie Structurale in Grenoble, France, and Professor Dan Tawfik, a pioneer in the field of protein evolution, at the Weizmann Institute of Science in Israel. Colin returned to Australia and was appointed an RSC lab head in 2011. Colin’s laboratory investigates the molecular and dynamic basis for protein function, protein evolution and protein engineering. Research highlights include: (1) mapping the changes in protein conformational landscapes during the evolution of new function (Nature Chemical Biology, 2016); (2) the engineering of a novel glycine sensor to follow neurotransmitter release in real-time (Nature Chemical Biology, 2018); (3) using ancestral protein reconstruction to recapitulate the emergence of enzymatic activity from a non-catalytic scaffold (Nature Chemical Biology, 2018); (4) revealing that the suboptimal activity of a designed enzyme originates from frequent sampling of non-catalytic states (Nature Communications, 2018); and (5) overcoming insecticide resistance through the development of a new class of inhibitors (Proceedings of the National Academy of Sciences USA, 2019). These compounds are currently under a commercialisation agreement.

Colin has published over 100 articles in top journals such as Nature Chemical Biology, Nature Immunology, Nature Communications, eLife and Proceedings of the National Academy of Sciences USA. He is the recipient of a 2011 Discovery Early Career Researcher Award, 2012 HFSP Young Investigator Award, 2014 ARC Future Fellowship, 2014 Tall Poppy and Act Tall Poppy of the Year, 2015 ACT Scientist of the Year and 2015 RACI Rennie Memorial Medal.


ASBMB Medallist and Awardee ProfilesThe SDR Scientific Education Award rewards outstanding achievement in education in biochemistry or molecular biology, especially innovation and creativity in education, with a view to fostering leadership in this important area of the Society’s objectives. The Award will enable the recipient to participate in an international conference with a significant focus on education, or to spend a period of time at another institution (in Australia or overseas) for the purposes of undertaking developments in education in biochemistry and molecular biology. The recipient will present a lecture within the Education Symposium at the ASBMB annual conference. Applicants must have been members of the Society for at least two years before the year in which the Award application is to be considered. The contribution to travel expenses is provided through the courtesy of SDR Scientific.

SDR Scientific Education AwardNirma Samarawickrema

The educator I am today is because of my students. I love my teaching and enjoy my research and each enriches the other, adding value to both. Involving my students and peers, and integrating learning into this mix is what fires me as an educator!

My learning followed a traditional path of completing my BSc and MSc at the Australian National University and PhD in Molecular Parasitology/Biochemistry at the University of Queensland. I began my teaching career as a demonstrator at Kelaniya University, Sri Lanka. My students were school leavers from diverse socioeconomic backgrounds, many undertaking urban relocation and experiencing study in English (a second language) for the first time. As a new academic, my approach was to convey content knowledge and dictate the learning process. However, I soon learnt that my students found Biochemistry ‘difficult’ and irrelevant to their medical careers. This feedback meant I had to find ways of actively engaging students and embedding career-connections in their learning so that they were scaffolded to succeed and become empowered to persist beyond first year. As a senior lecturer at Monash University, Australia, I continue to teach first year subjects. I coordinate units and teach Biochemistry to multiple student cohorts (medical, biomedical, nutrition and science) across the medical and science faculties. My classes are large (>700), where students come from diverse backgrounds, capabilities, expectations, with many transitioning to university from other types of work.

Mindful of this diversity in my classes, I have focused my teaching to facilitate lifelong learning in students through partnerships. My first-year students are lively, eager to learn and keen to enjoy university life. I have discovered that their voice is a rich resource in the classroom – they each have a unique perspective to offer. This learning has transformed my teaching as I have increasingly grown to consider my students as my partners in teaching and learning.

In the last ten years as I transitioned to be an education-focused academic, I broadened my research focus to include the scholarship of teaching and learning (SoTL), while retaining some aspect of my disciplinary research. I have drawn on my disciplinary research on human papillomavirus and cervical cancer to develop learning activities now integrated into the curricula and utilised it to initiate my research interests in teaching and learning. My SoTL research focus is broadly on partnerships (students, teaching associates and academics) and on building assessment literacy that enhance teaching and learning. In recognition of demonstrating sustained leadership and innovation in education, I was elected a Fellow of the Monash Education Academy and Fellow of the Higher Education Research and Development Society of Australasia.

I love teaching Biochemistry to young students. As rewarding as it is, I feel deeply accountable as I foster the biochemists of future generations.


ASBMB Medallist and Awardee ProfilesThe Eppendorf Edman ECR Award is awarded to an ASBMB member with no more than seven years postdoctoral experience (or equivalent taking any career disruption into account), in recognition of their outstanding research work. The Award provides funds to assist the recipient to attend an overseas conference in a field associated with biochemistry or molecular biology or to visit briefly a research laboratory in Australia or elsewhere to access specialised equipment or to learn new research techniques. The recipient will present a lecture within a symposium at the ASBMB annual conference. Applicants must have been members of the Society for at least two years before the year in which the application is to be considered, or must have taken out a three year membership in the year of the application. The contribution to travel expenses is provided through the courtesy of Eppendorf South Pacific.

Eppendorf Edman ECR AwardSi Ming Man

Si Ming completed a Bachelor of Medical Science (Hons I, University Medal) at UNSW Sydney. During his Honours year, Si Ming investigated the role of mucus-associated bacteria in children with inflammatory bowel diseases. His interests in host–pathogen interaction inspired his move to the UK, where he completed his PhD at the University of Cambridge in 2013 under the supervision of Professor Clare Bryant. During his PhD, he studied macrophage responses to the foodborne pathogen Salmonella spp. and generated two first-author publications in Proceedings of the National Academy of Sciences USA and a first-author publication in the Journal of Immunology. With the support of an NHMRC RG Menzies Early Career Fellowship, Si Ming moved to Memphis, Tennessee, USA, where he completed his postdoctoral training at St Jude Children’s Research Hospital under the mentorship of Dr Thirumala-Devi Kanneganti. During this time, Si Ming and his colleagues identified (1) a role for disease-fighting proteins in liberating microbial ligands to drive activation of innate immunity (Cell, 2016; Nature Immunology, 2015); (2) the activation mechanisms of immune receptors in cancer (Cell, 2015; Nature, 2016). Si Ming returned to Australia to establish his lab at the Australian National University in 2017. He is now a Professor and NHMRC RD Wright Biomedical Fellow. His laboratory focuses on understanding the role of innate immunity in the host defense against infectious diseases and the development of cancer (Nature Microbiology 2019, Nature Communications, 2020).

Si Ming was a recipient of the Pfizer-Showell Award (2019) and the Thermo Fisher Trainee Achievement Award (2016) from the American Association of Immunologists, the Milstein Young Investigator Award from the International Cytokine and Interferon Society (2016), the Jim Pittard Early Career Award from the Australian Society for Microbiology (2017), the Royal Society of NSW Edgeworth David Medal (2019), an NHMRC Research Excellence Award for the highest-ranked Early Career Fellowship (2015) and an NHMRC Research Excellence Award for the highest-ranked Career Development Fellowship Biomedical Level 1 (2019). He also received the 2019 Commonwealth Health Minister’s Medal for Excellence in Health and Medical Research.


ASBMB Medallist and Awardee ProfilesThe Boomerang Award is offered to an outstanding expatriate Australian biochemist or molecular biologist to provide an opportunity to return to Australia to present their work in a Symposium at the annual ASBMB conference and to give seminars at universities or research institutes in at least one other Australian city. The Award is intended to provide the awardee with exposure in Australia and to facilitate interactions with local researchers. Applicants must have been a member of a recognised Australian scientific society for at least two years, or must have taken out a three year membership in the year of the application, and awarded their PhD not more than ten years prior to the closing date (or equivalent taking any career disruption into account). The contribution to travel expenses is provided by ASBMB.

Boomerang AwardMatthew Doyle

After completing his BSc (Biotechnology) in 2011 at the University of Adelaide, Dr Matt Doyle was fast-tracked into postgraduate research through the award of a ‘No Honours’ scholarship. Working with Associate Professor Renato Morona at the Research Centre for Infectious Diseases, Matt developed methods to investigate how outer membrane proteins (OMPs) of Gram-negative bacteria are transported to, and/or translocated across, the bacterial cell surface. For this work he used a model OMP called IcsA, which is an essential virulence factor for Shigella species to cause bleeding diarrhoea in humans. He identified motifs within IcsA that drive correct membrane localisation and are conserved in thousands of OMPs across many Gram-negative pathogens. Matt’s PhD studies contributed towards six research articles and attracted multiple awards including the 2014 Adelaide Protein Group Speaker Award and the University Doctoral Research Medal.

After completing his PhD in 2015, Matt was awarded a National Institutes of Health (NIH) Visiting Fellowship to conduct postdoctoral training in the laboratory of Dr Harris Bernstein in the USA. At the NIH, Matt has designed the first experimental system that can controllably trap new OMPs in the final stages of membrane integration and folding in cells. By combining in vivo protein–protein disulphide crosslinking approaches, he mapped the interactions of a new OMP with the folding machinery known as the BAM complex. BAM contains protein subunits conserved in all Gram-negative bacteria as well as organelles such as mitochondria and chloroplasts. This work resulted in a new model for OMP membrane integration and was published in 2019 in Nature Communications. Apart from his research at the NIH, Matt has also been recognised for his mentoring through a 2018 NIH Research Mentor Award, which provided mentoring training as well as salary for a summer intern from a socioeconomically disadvantaged background.

Matt remains captivated by the study of OMP biogenesis and argues that the information is critical for the design of new antibiotics, a better understanding of how bacteria cause disease and the improvement of bioprocessing technologies. He attributes his past successes to a multidisciplinary approach to experiment design (e.g. biochemistry, structural biology, and microbiology). Matt wishes to eventually return to Australia to continue his research and pursue an academic career.

Matt thanks the ASBMB for this amazing opportunity to share new findings at an ASBMB meeting and to visit laboratories in Australian cities including Canberra (Dr Denisse Leyton, Australian National University) and Melbourne (Professor Trevor Lithgow, Monash University).


ASBMB Fellowship ProfilesThe ASBMB Fellowships are awarded annually to biochemists or molecular biologists, in their early career and normally resident in Australia, in recognition of their outstanding work in an area of biochemistry and molecular biology.The Fellowships provide funds to assist the recipient to attend an overseas conference in a field associated with biochemistry or molecular biology or to briefly visit a research laboratory in Australia or elsewhere to access specialised equipment or to learn new research techniques.Applicants must be at least in the second year of PhD training and not more than two years subsequent to the award of the PhD degree. Applicants must have been members of the Society for least one year immediately prior to application.

Amy Baxter – recipient of the Fred Collins award for the most outstanding ASBMB Fellowship applicant

Dr Amy Baxter completed a Bachelor of Human Nutrition in 2009 at La Trobe University in Bundoora, Victoria. She continued on at La Trobe, completing her Honours year in 2010 and PhD from 2012–2017 (including maternity leave periods for each of her two children, now aged four and seven) in the Department of Biochemistry and Genetics under Professor Mark Hulett. During this time, Amy investigated the molecular basis of tumour cell membrane disruption by plant defensins, discovering that defensins can bind membrane phosphoinositides in target cells and form oligomeric structures to mediate cell lysis. Her research made a significant impact in the innate immunity field, reflected in the ten papers published during her PhD, including in eLife and Cell Death and Differentiation, generating over 300 citations. In 2018, Amy was awarded an NHMRC Peter Doherty Early Career Fellowship to examine the mechanism and functions of extracellular vesicles formation during cell death, which she is currently undertaking under the supervision of Associate Professor Ivan Poon at the La Trobe Institute for Molecular Science (LIMS). She is currently investigating the roles of apoptotic cell disassembly and clearance in the context of vascular inflammation. Amy’s achievements, both during her PhD and since, have been recognised through her nomination for several research awards including the La Trobe University Nancy Millis Medal for Outstanding Theses (2017), Victorian Premier’s Award for Health and Medical Research (2019 Finalist, Basic Science category) and La Trobe University ECR Research Excellence Award (2019). Amy was scheduled to present her recent findings at the Gordon Cell Death Conference in Ventura, California, in June 2020.

Steffi CheungDr Steffi Cheung completed her Bachelor in Science (Honours) at the University

of Melbourne in 2014. She was awarded the MIRS and MIFRS scholarships by the University of Melbourne to undertake her PhD studies at the St Vincent’s Institute of Medical Research/Department of Biochemistry and Molecular Biology at the University of Melbourne under the mentorship of Professor Michael Parker in 2015. Her doctoral studies focussed on studying the signalling mechanism of the beta common family of cytokines, where she employed various biophysical techniques to complement her structural biology studies. She was awarded her doctoral degree in 2019, resulting in four publications. Her performance was also recognised by several awards, including the 2018 Sawyer Medal recognising her exceptional scientific contribution during her doctoral studies in the Department of Biochemistry and Molecular Biology at the University of Melbourne and the 2017 International Union of Crystallography Young Scientist Award, amongst others. She presents her work at local and international conferences, being invited to present her doctoral work at the CRYSTAL32/AsCA2018 conference and being awarded the 42nd International Lorne Protein Structure and Function Poster Prize. Steffi is now a postdoctoral researcher in the Structural Biology and Computational Design laboratory at the Bio21 Institute.

The ASBMB Fellowship was to give Steffi the opportunity to attend the 25th Congress of the IUCr assembly, Prague, Czech Republic, to help diversify her structural biology skills.


ASBMB Fellowship ProfilesAnukriti Mathur

Anukriti is a third year PhD student at the Australian National University under the supervision of Professor Si Ming Man. Her PhD project focuses on understanding the molecular mechanism of bacterial toxins in inducing cell death and inflammation. Her research identified two multicomponent bacterial toxins assembled in a specific and linear order on the mammalian cell membrane to form a lytic pore, to activate the immune sensor. These findings have been published in Nature Microbiology and Nature Communications, with Anukriti as a first/co-first author. She has published two review articles in Microbiology and Molecular Biology Reviews and Journal of Leukocyte Biology.

Anukriti completed her Bachelor of Technology in Biotechnology at Amity University, India, in 2010. She received a Master of Engineering in Biotechnology from the Birla Institute of Technology & Science, Pilani Campus, India, in 2016. In 2015, she was awarded a Khorana fellowship by the Government of India which allowed her to conduct a research project at the Harvard Medical School, USA. Anukriti’s doctoral work has been recognised by a Gretel and Gordon Bootes Medical Research Foundation grant award, an American Association of Immunologists trainee poster award, an International Cytokine and Interferon Society Sidney & Joan Pestka Graduate Award, an Australian Society for Microbiology Nancy Millis student award and an International Association of Inflammation Societies Young Investigator Award.

This ASBMB Fellowship was to give Anukriti an opportunity to present her research findings at the American Association of Immunologists annual meeting in Honolulu, USA, and meet potential employers and collaborators.

Mengjie Hu Dr Mengjie Hu completed her Bachelor of Science at the University of Melbourne, followed

by a Masters degree in Biomedical Science in 2012, where she investigated mitochondrial biochemistry with Associate Professor Marie Bogoyevitch at the Bio21 Institute, leading to a first author publication in Biochemical Journal. Mengjie subsequently worked as a Research Scientist and Project Team Leader in a multinational pharmaceutical company. In 2014, she commenced her PhD at the University of Melbourne with the support of Melbourne International Research and International Fee Remission Scholarships in the labs of Associate Professor Marie Bogoyevitch and Professor David Jans (Monash University). There, she investigated how infection by respiratory syncytial virus (RSV) impacts mitochondrial morphology and function, and conversely how manipulation of mitochondrial function can impact RSV infection. Her work developed a new therapeutic approach to combating RSV infection, culminating in first author publications in Biochemical and Biophysical Research Communications, eLife, Cells, and a comprehensive review in Physiological Reviews, as well as several awards in 3 Minute Thesis Competitions. Mengjie was awarded her PhD in 2019 along with the Sawyer Medal from the Department of Biochemistry and Molecular Biology at the University of Melbourne in recognition of her outstanding research achievements. Since then, Mengjie has worked on a number of projects involving other infectious viruses including Dengue and Zika, and has recently embarked on a new journey in clinical research.

This ASBMB Fellowship was to give Mengjie an opportunity to present her findings at the 16th World Congress on Virology, Emerging Diseases & Vaccines in Italy, and then visit several eminent laboratories at Imperial College in London.

Editor’s note: What a fitting conference and location in light of the current COVID-19 pandemic. There will certainly be lots of new data to discuss when this conference is rescheduled.


Science meets Parliament 2019

‘You could be the best violinist in the world, but if you’re in a soundproof room, it is a waste.’ Winthrop Professor Fiona Wood’s opening address resonated with a room full of STEM experts from across the nation, kicking off Science meets Parliament 2019. The annual Science and Technology event celebrated its 20th anniversary last year, gathering STEM professionals for a two-day event with the Australian Parliament. The event is designed to educate STEM researchers about policy and governance, and connect researchers with parliamentarians to talk about science and its role in Australia’s health, environment, wealth and wellbeing. The ASBMB, an affiliate of Science Technology Australia, sponsored us (Vanessa Vongsouthi, ANU PhD candidate and ASBMB member, and Dr Matthew Johnson, ASBMB’s ACT State Representative) to attend the event and communicate our experience.

As per previous Science meets Parliament events, day one was aimed to educate attendees about the inner workings of Parliament, and prepare everyone for their meetings with parliamentarians using a range of eminent speakers and workshops. Science meets Parliament is all about communicating and networking and while sitting at round tables with delegates from across STEM, we had to concisely introduce ourselves and say what we do, all within one minute. The diversity of attendees was immediately apparent – museum curators, representatives from public policy think tanks, science commentators and biotech researchers, to name a few. For many researchers, who are accustomed to networking at subject specific conferences, this environment was already a welcome step outside our comfort zones. In her opening address, Professor

Wood gave an inspirational speech of her experience of translational research and how it can be used to improve the treatment of burns victims. Professor Wood’s story exemplified how basic research can be translated into real health outcomes with determination and perseverance. Australia’s Chief Scientist, Professor Alan Finkel, and New Zealand’s former Chief Science Advisor, Professor Gary Evans, spoke about their experience advocating for science and technology in Parliament. Professor Finkel talked specifically about the role that Australia might play in the production of clean hydrogen fuel for industry both in Australia and abroad, as opposed to the fossil fuel exports that the Australian government currently supports. Discussion was centred on the role of science in advising public policy, in the face of a growing presence of an anti-science culture in Australian politics.

Science meets Parliament offers two tracks, one geared for first time attendees, another for returning veterans. As this was our first time, we attended track one, which started with the ‘New to Canberra’ panel discussion featuring Paul Osborne (Bureau Chief and Journalist), Dr Sarah Pearson (Chief Scientist for Department of Foreign Affairs) and Sarah Cullens (Principle Consultant for Nexus Public Affairs). The session detailed how the media, lobby groups, public service, and advocacy groups influence government. Each panellist gave a detailed account of how their profession impacts government policy, and advice on how representatives from STEM can do the same. How a message is portrayed is as important as the message itself; scientists are often guilty of communicating with too much jargon, for too long and being too abstract. For members of Parliament, who primarily deal in votes, making your ideas real and relevant to them and their electorate is important to getting your message across. Fortunately, we had ample help and time to prepare our pitches. In the session ‘Practicing your Pitch’, Dr Will Grant and Dr Rod Lamberts gave us the tools to ditch the jargon and simplify our science. In one exercise, we iteratively distilled our pitch down from several minutes to as little as ten seconds. It was amazing to see how creative people in STEM can be with their pitches when time was restricted. The session was a fantastic experience for communication that geared us up for the networking events that followed.

Our first chance to meet Senators and Parliamentarians was at the ANSTO sponsored Gala Dinner held in the Great Hall. Our evening, hosted by SCOPE TV presenter, Lee Constable, provided a great opportunity to practice our networking skills. Unfortunately, the parliamentarians expected to sit at our particular tables were unable to attend. However, it was fascinating to meet people who work in different STEM-related jobs, many of which we

Matthew Johnson and Vanessa Vongsouthi report on SmP2019

From left: Trent Zimmerman MP, Alexandra Thomson, Kristine McGrath and Matthew Johnson.


Science meets Parliament 2019

didn’t realise existed. During dinner, we heard from The Hon Karen Andrews MP (Minster for Industry, Science and Technology) and The Hon Brendan O’Connor MP (Shadow Minister for Employment and Industry, Science, Small and Family Business) about their visions for STEM in Australia.

Day two of Science meets Parliament was largely about the personal meetings with an assigned parliamentarian. We were assigned to meet Trent Zimmerman MP and Graham Perrett MP (Shadow Assistant Minister for Education and Training). Mr Zimmerman is a Liberal MP

for North Sydney who supports same-sex marriage and recently the full legalisation of e-cigarettes. Despite a busy schedule, Mr Zimmerman met with myself and two other STEM representatives. Mr Zimmerman was very engaging and interested in our various areas of research, and we had a short discussion regarding my research on resistance to antibiotics and the development of novel treatments. Unfortunately, the bells rang and parliamentary business cut our meeting short. Mr Perrett is a Labor MP for Moreton, teacher, lawyer and author. He met with Vanessa and four other delegates, taking the time out of his day to have an exciting discussion about STEM teaching in Australia, graphene water-filtering technology, and Vanessa’s research on plastic-degrading enzymes. Science meets Parliament concluded with a panel discussion with Ministers from both sides of politics answering questions from the STEM community. The lack of science in policy making was a prominent topic. The blame was placed on the STEM community for not communicating to politicians and the wider community clearly enough. On the topic of climate change, we were reassured that climate change denial is not prevalent in Australian politics and that the discussion has moved on to what we need to do about it. However, considering this panel discussion and the recent push by parliamentarians for a science watchdog, it seems that communication between STEM, the public and Parliament is more important than ever.

[email protected]@anu.edu.au

From left: Tim Rawling, Vanessa Vongsouthi,Erika Duan, Leanne Cameron, Timothyvan der Laan and Graham Perrett MP.

The Australian Academy of Science established the Boden Conference Award to fund small specialist conferences in the biological sciences with the generous support of the late Dr Alex Boden AO FAA. These conferences, which usually run for about two days, bring together researchers working in rapidly advancing fields to discuss current advances and problems. A sum of up to $10,000 is provided, and organisers are encouraged to seek additional funding from other sources. One conference is funded annually.Applications close: 9:00am 1 June 2020Further information: Boden Conferences page on AAS websiteContact: [email protected] or (02) 6201 9407

Call for Expressions of Intent – AAS Boden Conference Award

https://www.science.org.au/supporting-science/awards-and-opportunities/boden-research-conferences


The Sydney Protein Group (SPG) is comprised of scientists and students from academia, hospitals and industry who are interested in all aspects of protein science research. Founded in the 1980s, the SPG promotes protein science, and supports students and early- and mid-career researchers (EMCRs) in the field. With the help of funding from the ASBMB and trade partners, SPG organises a number of events throughout the year, with an emphasis on providing opportunities for students and EMCRs to present their research and enhance their network at high quality scientific conferences.

Over the past year, the SPG has organised a number of local and national events. One of the initiatives of the ASBMB is to provide a SIG-sponsored presentation at ComBio/ASBMB conferences for a promising early-career researcher. This year, James Walshe from the Victor Chang Cardiac Research Institute was awarded the scholarship and presented his cryo-EM research into E. coli ATP synthase at ASBMB 2019 in Fremantle. At this meeting, the SPG also hosted a SIG session to showcase the research being conducted by protein scientists from across New South Wales, which was sponsored by the ASBMB. The session saw recent highlights from Chandrika Deshpande (Centenary Institute) on the role of calcium for metal efflux by ferroportin transporters; Karishma Patel (University of Sydney) on the structural diversity of high-affinity cyclic peptides that inhibit bromodomains; Bishnu Paudel (University of Wollongong) on the activity of human telomerase on G-quadruplexes at single-molecule resolution; and Emma Sierecki (UNSW) on the different interactions of the Mediator complex.

One of the most anticipated nights on the SPG calendar is the annual Thompson Prize, named in honour of the eminent local protein scientist, E.O.P. (Ted) Thompson. Students are encouraged to submit abstracts to secure a speaking spot, and the best oral presentation of the night is awarded the prestigious Thompson Prize. The 28th Annual Thompson Prize was held in conjunction with a half-day symposium on 22 November 2019 at the University of Sydney, hosted by Joel Mackay and Jason Low. The evening showcased some of the high calibre research being conducted by students from all around the greater Sydney area, and was well attended by the SPG community.

Harry Rathbone (UNSW) described his work on phycobiliproteins and how the cryptophyte Hemiselmis andersenii have adapted these proteins to capture various wavelengths of light. Next, Sayantani Chatterjee

(Macquarie University) presented her work on the pre-dominance of paucimannosylation in human cancers, and its potential use as a cancer biomarker. Yicheng Jessica Zhong (University of Sydney) detailed her single molecule work probing the mechanism by which CHD4 enables nucleosomes to slide during chromatin remodelling. The penultimate speaker, Yi Zeng (VCCRI), showcased his cryo-EM structures of archeal TF55 chaperonin from Sulfolobus solfataricus, suggesting that the protein may form filaments to regulate chaperone activity. Lastly, Ngee Kiat Jake Chua (UNSW) described his PhD project looking at the regulation of squalene monooxygenase – an important player in cholesterol homeostasis.

The symposium guest speakers, international NMR spectroscopists Ad Bax, Rasmus Linser and Kevin Gardner, were judges for the event. Jessica Zhong was announced as winner of the 2019 Thompson Prize. Conference travel awards were also given to three students, in recognition of their research achievements so far. The ATA Scientific, ANSTO and Greg Ralston Memorial Prize travel awards were awarded to Charlotte Franck (University of Sydney), Serene El-Kamand (Western Sydney University) and Teegan Lawson (Western Sydney University), respectively, to attend the Lorne Proteins or Proteomics Meetings.

The SPG Annual General Meeting was held immediately after the Thompson Prize ceremony and, after almost ten years of leading the SPG community, Liza Cubbedu (President) and Roland Gamsjaeger (Committee Member/Webmaster) stepped down from the leadership team. We cannot thank Liza and Roland enough for their tireless work in supporting SPG members and promoting local protein science over the years. The quality of speakers at the Thompson Prize event is a testament to their hard work and the reputation of the SPG initiative. Tara Christie (University of Sydney) and Alastair Stewart (VCCRI) were then elected as President and Committee Member/Webmaster, respectively. They are committed

Sydney Protein Group: an ASBMB Special Interest Group

Jessica Zhong(left) receives the

2019 Thompson Prize from SPG President,

Liza Cubbedu.


to growing a collaborative and productive network of protein scientists.

To kick off 2020, a mini-symposium was held in February at the University of Sydney. The afternoon featured talks from distinguished researchers Antoine van Oijen (University of Wollongong), Marc Wilkins (UNSW), Margie Sunde (University of Sydney) and Andrei Lupas (Max Planck Institute for Developmental Biology, Germany). This event was well received by the community, as evidenced by the large turnout and lively discussions following the talks. We thank ASBMB and

AXT Pty Ltd for supporting this event, which enabled SPG to put together such an impressive and stimulating program for the local protein community. The SPG looks forward to another great year of hosting protein science events and supporting the fantastic research being conducted by local protein scientists.

Tara Christie (President) and Jason Low (Secretary)Sydney Protein Group

https://www.asbmb.org.au/ special-interest-groups/sydney-protein-group/

Sydney Protein Group: an ASBMB Special Interest Group

Nominations are called for the following positions on the Council of the Australian Society for Biochemistry and Molecular Biology Inc for 2021: Secretary, Treasurer, Editor, Secretary for Sustaining Members and State Representatives.

President J MackayPresident Elect J MatthewsSecretary B Forbes §Treasurer M Kvansakul #Editor T Soares da Costa #Education Representative N Samarawickrema #Secretary for Sustaining Members S Jay #

ACT M Johnson §NSW K Quinlan §Vic E Lee §Qld B Schulz §SA M Pittman #Tas K Brettingham-Moore § WA M Murcha §

Nomination forms are available on the ASBMB website. Nominations for all vacant positions must be signed and seconded by members of the Society. The nominations must be signed by the nominee to indicate his/her willingness to stand. If more than one nomination is received for any position, a ballot will be held at the Annual General Meeting. All members will be notified of any elections and members not attending the Annual General Meeting may submit a proxy form available from the Secretary.

NOMINATIONS MUST REACH THE SECRETARY BY AGM IN SEPTEMBER/OCTOBER 2020 (DETAILS TO BE ADVISED).

# Eligible for re-election

§ Position open

The ASBMB Council for the period 1 January 2020 to 31 December 2020 is composed of the following members:

Representatives for:

Election of Council 2021

mailto:https://www.asbmb.org.au/%0Aspecial-interest-groups/sydney-protein-group/?subject=

mailto:https://www.asbmb.org.au/%0Aspecial-interest-groups/sydney-protein-group/?subject=


Biochemistry on StageSystematic Absences

Terry Mulhern, Department of Biochemistryand Molecular Biology, University of Melbourne

In October 2019, deep underground in the bowels of the University of Melbourne’s Bio21 Institute, a dozen VIPs are clustered around a scientific instrument resembling a large squat refrigerator. These aren’t overseas scientists, entrepreneurs or politicians. They are actors. This is the cast of the Melbourne Theatre Company’s production of Anna Ziegler’s play, Photograph 51.

Since 2010, Photograph 51 has been performed to packed houses from New York to Stockholm. In 2015, it played in London’s West End with Nicole Kidman in the leading role. Pamela Rabe is to direct its run at the Fairfax Theatre in the Melbourne Arts Centre (1 November–14 December 2019). The cast, including Nadine Garner (The Doctor Blake Mysteries), are here to school themselves in the dark arts of X-ray diffraction and to hear the perspectives of real scientists on the motivations, rivalries and sexual politics at the heart of the story they will portray.

The group listen intently, as crystallographer Megan Maher explains the operation of the X-ray diffractometer. The bottom half, containing the X-ray generator, is completely enclosed by metal shielding, but a window in the top half reveals an assembly of gleaming metal devices. Several probe-like appendages converge to a single point. Here, a narrow powerful beam of X-rays is focussed onto a tiny crystal of biological material. The X-rays impinge on the crystal and are then scattered in all directions by the ordered crystalline lattice of molecules. The emergent waves of energy interfere with each other constructively and destructively. In some directions, they add together to become more intense but in other directions they annihilate each other and vanish. When the diffracted beams hit the detector,

the result is complex and beautiful. Geometric patterns form composed of lines of spots of varying intensity with occasional gaps – so called ‘systematic absences’. In days gone by, these images were captured on photographic film. Photograph 51 was the understated name given in 1952 by the trailblazing female scientist Rosalind Franklin, to the most famous X-ray diffraction image ever captured.

In a dank basement at King’s College in post-second world war London, Rosalind Franklin used a much more rudimentary diffractometer to record photograph 51. Time and time again, she and PhD student Raymond Gosling painstakingly aligned semicrystalline fibres of DNA in the X-ray beam and recorded photographs. By controlling the humidity inside the diffractometer, Franklin was able to tease apart the contributions from the A and B forms of DNA. Photograph 51 was recorded under higher humidity, which favours the more hydrated and elongated B form that more closely resembles the state of DNA in living cells.

Photograph 51 subsequently fell into the hands of a brash young American working at Cambridge University, James D Watson. It contained the key information that allowed Watson and his older English colleague Francis Crick to propose their famous double helix structure of DNA. Their model for DNA was elegant in its simplicity and earth shattering in its significance. This great leap forward paved the way for the genomics revolution that we are immersed in today. In recognition of this discovery, Watson, Crick and Franklin’s male colleague, Maurice Wilkins, received the 1962 Nobel Prize for Medicine. But not Rosalind Franklin. She died of ovarian cancer in 1958. Ironically, Franklin’s premature death averted a controversy that was brewing. Watson and Crick’s place in history was assured, but either Franklin or Wilkins would have had to miss out. Nobel Prizes can be shared by no more than three individuals.

The intellectual and emotional conflict of the fraught relationships still fascinates us, more than 70 years

Photograph 51.

Nadine Garner as Rosalind Franklin andGig Clarke as Ray Gosling. Photo: Pia Johnson.


Biochemistry on Stage

on. The way Watson and Crick learned the details of Franklin’s experiments and how Watson obtained her diffraction pattern speak volumes about the attitudes towards women in science and society of the time.

Back upstairs in the Bio21 boardroom, we show the cast 3D animations of DNA molecules and talk about the meaning of different geometric features of photograph 51. We explain how the X shape indicates helical structure and that the layer lines define repeating distances. The systematic absence of the fourth layer line indicates that the two twisted DNA strands are offset by 3/8 of a turn. This asymmetry gives rise to the major groove and minor groove in the structure where (as we now know) protein machines can nuzzle into the structure and read its blueprint.

We are bombarded with questions, both technical and about what it is like being a scientist. The most telling was, ‘Do you think what Watson and Crick did was right?’ The four scientists in the room, geneticist

Karen Day, molecular biologist Heather Verkade and structural biologists Megan Maher and I momentarily pause and then, unanimously agree: ‘No’. What they did was wrong. And it is not a matter of different standards for different times. It was wrong then and it is still wrong now. In Cambridge, Max Perutz improperly gave a report on Franklin’s work to Lawrence Bragg, which then found its way into the hands of Watson and Crick. Although argument has ensued for decades, it is doubtful that Watson and Crick should ever have been allowed to see it. At King’s College, Wilkins then overstepped his authority by handing Watson photograph 51 without consulting Franklin. Imagine how you would feel if your grant application containing unpublish data was ‘shared’ with your competitors; and then to top it off, a senior colleague gifts them your raw data behind your back?

The acknowledgements section of a thesis or paper can be fascinating and revealing. Like diffraction patterns, there is information in what is both present and missing. Three papers, authored by Photograph 51’s key protagonists, appeared back-to-back in the April 1953 issue of Nature. Watson and Crick acknowledge having been ‘stimulated by a knowledge of the general nature of the unpublished experimental results and ideas’ of Wilkins and Franklin (1). In his paper, Wilkins thanks Watson and Crick for ‘stimulation’ and Franklin for ‘discussion’ (2). Tellingly, Rosalind Franklin is ‘grateful’ to just Wilkins and Crick (3). James D. Watson’s name is a systematic absence.

References1. Watson JD, Crick FH (1953) Nature 171:737–738.2. Wilkins MHF, Stokes AR, Wilson HR (1953) Nature

171:738–740.3. Franklin RE, Gosling RG (1953) Nature 171:740–741.

Associate Professor Terry Mulhern is the Director of Teaching and Learning for Biochemistry and

Molecular Biology in the School of Biomedical Sciences at the

University of [email protected]

Rosalind Franklin on vacation in Tuscany, spring 1950.Photo: US National Library of Medicine.

Nobel Prize winners at the ceremony in Stockholm, Sweden, 1962. From left: biophysicist Francis Crick, biophysicist Maurice Wilkins, writer John Steinbeck, geneticist James Watson, biochemist Max Perutzand biochemist John Kendrew. Photo: Granger.

Acknowledgements section fromRosalind Franklin’s April 1953 Nature paper (3).


In this reflection, I will highlight some of my experiences which may be helpful for early career scientists to ensure you enjoy what you are doing and give yourself the best chance of success. The issues that have been striking for me have been the opportunity to work across a number of different disciplines and to interact with many people both locally and from different parts of the globe. Collaborations are the key to an enjoyable research career and optimising outcomes and opportunities.

Early daysI grew up in the conservative Melbourne environment

of the 50s and early 60s. International travel was uncommon. My parents, who hadn’t travelled extensively, had the opportunity through my father’s work in the paper manufacturing industry, to go overseas for eight months when I was seven years old. The six of us kids were farmed out to various relatives and friends around Victoria for this period and I tracked the movements of my parents across Europe and North America. It was all a mystery, but travel became implanted in my psyche as a must for my future.

I had excellent maths teachers at school, but other areas of science teaching were less inspiring. Although I had no exposure to biology at school (it was not deemed a subject for an all boys’ school!), I found life sciences fascinating. Basic genetics made a deep impression. I read The Double Helix by James Watson (1969) and found the creative drive and world of discovery thrilling. The idea of a life chasing intellectual pursuits, akin to the ethereal Glass Bead Game by Herman Hesse (1946), involving an abstract game of a synthesis of arts and science, which I read several times, was very appealing.

Finding my way into research I studied Science at the University of Melbourne

without a clear grasp on what I wanted to do. Biochemistry and Microbiology (with Immunology integrated in those days) were my majors. Class sizes were small and practical classes were numerous. The logic of biochemistry was satisfying; the architecture of organisms and mechanisms for survival and adaption captivated me. The seeds for a future molecular cell biologist as I now reflect. Also, microbial genetics was just beginning, and William Hayes’s book Genetics of Bacteria and their Viruses (1969) described the fantastic power of bacteriophages and conjugation systems in

genetic analysis. The conceptual puzzle of immunology was fun but at that stage cellular immunology was like a house of cards. The doors of research were opened by a summer vacation studentship at CSIRO Division of Protein Chemistry with Lindsay Sparrow and Colin Ward. I found that purifying proteins could be fun.

I was an Honours student with Nancy Millis in the Microbiology Department at the University of Melbourne, researching an industrial microbiology problem. Nancy was a notable pioneer in biotechnology in Australia and one of the first women to be appointed to Professor. The people and environment were inspiring but I came to realise that I was more interested in molecules. Then, via the connection as summer student, I was employed at CSIRO for two years as a research assistant with Michael Jermyn, an eclectic scientist and polymath. Mike introduced me to sugars and lectins. And by a stroke of luck, Mike had a collaboration at Melbourne University with Adrienne Clarke and Bruce Knox in the School of Botany. I then joined their lab as a PhD student defining the structure and function of polysaccharides involved in fertilisation of flowering plants. The ecologists in the Botany School were alarmed that a PhD student in their department did not have a major in botany!

It was the early days of Adrienne’s Clarke’s lab; she went on to become a world leader in the field of self-incompatibility in flowering plants and the chemistry of complex carbohydrates, as well as founding a significant biotechnology company. Adrienne cultivated a strong team approach by nurturing interactions and collaborations, with minimal hierarchy. I worked alongside protein biochemists, optical and electron microscopists and geneticists. Adrienne often reminded us of the central scientific questions being investigated and, if expert advice was needed beyond our sphere, we were encouraged to venture out of our comfort zone. This multidisciplinary approach had a lasting influence for me on how science ought to be done.

There was close association with the marine biologists in the department and I was very fortunate to hitch a memorable ride to Heron Island research station on their field trips on two separate occasions. When opportunity knocks, take it! I learnt to scuba dive and we collected Tridacna maxima clams from the reef (with permits!). Back in the lab, we purified a lectin from the Tridacna haemolymph that was then used for a one-step affinity purification of an arabinogalactan polysaccharide. So, my trip to Heron saved me about a year’s work purifying

Unexpected Journeys Through DifferentResearch Lands and Scientific Families

Great Expectations

Paul Gleeson is the former Head of the Department of Biochemistry at the University of Melbourne. He is passionate cell biologist and advocate for basic science. His career has spanned over 35 years.


a difficult polysaccharide. We closely collaborated with Bruce Stone’s lab at La Trobe University. Fellow students between the two labs included Tony Bacic and Malcolm McConville; we became lifelong friends and years later we would find ourselves either supervising or be supervised by each other in leadership roles. At the time, never in my wildest imagination!

Postdoctoral experiencesFollowing completion of my PhD in 1980, I became

interested in synthesis of glycoproteins and wanted to move to a lab working on animal systems. Through connections with Adrienne and Bruce Stone, I was offered a postdoc from Harry Schachter in Toronto. Considering that I had not met Harry nor visited his lab, it worked out amazingly well. However, I certainly would encourage any graduate student to go and visit their potential future labs and mentors. Harry was very generous and he knew everyone in the field. It was an exciting time in the glycoprotein synthesis field and my work resulted in the discovery of a Golgi-localised GlcNAc transferase involved in N-glycan synthesis of branched complex N-glycans, using mass spectrometry and NMR to characterise the products and enzyme specificity. As with my PhD work, I put in long hours at the lab but also used the opportunity to travel with my partner Christine: we explored Canada from east to west. Via Harry’s connections and generosity in supporting his ‘team’ members, I subsequently became the Australian representative for the International Glycoconjugate Organization (IGO) and then organised GLYCO-19 meeting in Cairns in 2007. Relationships evolve opportunities.

I was keen to also experience the science culture in UK and Europe. Colin Hughes at the time was one of the foremost glycobiologists in the UK and his work on the function of N-glycans, by generating and using lectin resistant mammalian cells, was attractive to me as I would gain experience in emerging cell biology

techniques. From Toronto, I then went to the National Institute of Medical Research at Mill Hill in London on a Beit Fellowship to work in Colin’s lab. Here, I expanded my work on carbohydrates and obtained experience in mammalian cell systems, generating lectin mutants, tracking toxins into intracellular endosomes, and characterising the total pool of N-glycans in mutant CHO cells with Jim Feeney using their newly installed 500 MHz NMR. The environment at Mill Hill was very conducive to meeting others; there was a bar in the institute where we would gather at the end of the day, and a squash court on site! I met many from outside the biochemistry division including developmental biologists, immunologists and parasitologists. I did not realise at the time but these networks had a strong impact on broadening my horizons.

In 1984, I returned to Bruce Stone and Geoff Fincher’s labs at La Trobe to learn recombinant DNA techniques and integrate back into the local science community. When I left Australia there were relatively few opportunities for a research career. Four years later it was buzzing, with new research institutes being established. New early career fellowship schemes were appearing. This is an important message in the cycles of research activity; it is hard to predict what the future holds in research funding and opportunities. The recent bushfires and coronavirus pandemic have raised the importance of science and scientists, in the general community.

Immunology comes into focusMy next piece of luck (in 1986) was an offer for a

three-year lectureship in the Department of Pathology and Immunology, Monash, at The Alfred hospital site, by the incoming head, Jim Goding. This unexpected appointment came from a chance presentation of my work from Mill Hill at a local meeting organised by Jim. He was keen to bring to his department people across a range of disciplines. It was a great environment to set up an independent lab as there were several young academic staff. I quickly realised that I would become isolated if I exclusively followed my previous research interests and my best option was to collaborate with others around the department. I become interested in the biochemical characterisation of autoantigens (gastric) with Ban-Hock Toh.

My lectures to students were initially focused on the biochemistry of immune molecules; staff also gave weekly tutorials to third year immunology students. This was a crash course for me in updating my immunology and I spent considerable effort in learning the field. It was the classic case of the blind leading the blind, but the focus gave me great insight into challenges for students to learn the complexity, uncertainty and sometimes contradictions in the immunology field. It demonstrated the incredible value of teaching alongside research.

Teaching extended my interests into cellular immunology of autoimmune diseases and, together with

Great Expectations

Paul on Heron Island with marine biologists in 1977.


Artist’s rendition of the Golgi apparatus.By Chloe Gleeson, Paul’s daughter.

the newly arrived Ian van Driel and Frank Carbone in the department, we delved into the world of autoreactive T cells and CD25+ regulatory T cells, which were new kids on the immune block. Studying autoimmunity provided a great challenge to all the underlying concepts in the field of immunology. The partnership with Ian was particularly important as we formed a joint team of an autoimmunity/gastric biology program that would go on to produce a series of papers and successful grants over more than two decades. Also, I was able to keep up my specific interests in the Golgi apparatus, where I exploited the environment and capitalised on screening and identifying autoantibodies from patients with systemic autoimmune diseases to map new Golgi components that ultimately led to defining trafficking pathways into and from the Golgi. Exposure to new fields enriches your research ideas in very unexpected ways.

Students and postdocs: choose wiselyI have been exceptionally fortunate with the quality of

PhD students and postdocs in my lab. All have been very talented and terrific people to work with. There is a temptation early on in your career to try to rapidly build up the group. Don’t! Choose wisely. Academic performance is just one measure. The individuals need to fit into the culture of your team and be able to interact well together. One misplaced individual will consume hours of your time to sort out the problems. I always include my lab team in the selection process by providing them the opportunity to meet the individuals (if not in person, by Skype) and taking on board their feedback. I am proud that all my PhD students have completed successfully. In addition to research, they have also gone off in a variety of different careers (for example, genetic counselling, IT, epidemiology, teaching). The stability of my group has been dramatically enhanced by a long-term research assistant, Fiona Houghton. Fiona has stuck by the lab for more than 20 years and has provided support for all in

the incoming students and postdocs and ensuring social events are maintained.

The move to the University of MelbourneI think moving environments is a good idea as it

refreshes. After many good years at Monash Pathology and Immunology, the administration ran into problems which permeated throughout the department. Suffice it to say that universities are not particularly good at fixing things up when they go wrong; it is largely up to the people at the coalface. Ironically, it was an experience that provided me with exceptional training for the future in what matters in helping to run a department. Later, I attended many leadership courses, but none matched the on-the-ground experience dealing with problems.

Luckily for us, the Department of Biochemistry at the University of Melbourne was looking to recruit two new staff. So, Ian and I applied as a joint team in 2001 and were successful, under the new departmental headship of Mary-Jane Gething. Little did we know at the time that two future heads of departments had just been appointed. The attraction was that the department was undergoing a generational change and that the future move into the soon to be constructed Bio21 Institute, driven by the outgoing Head, Dick Wettenhall. Bio21 would provide multidisciplinary opportunities, break down barriers and be in close proximity to industry. Our decision was about predicting where that environment would lead to in the longer term. There were major challenges in the move to bring many lines of mice into the facility and try to keep the needs of the individuals in the lab moving along. The challenges were greatly softened by having both of us working to sort out the problems, with the great support from the departmental animal technician, Max Walker.

We moved into Bio21 in 2004 and the research with Ian on autoreactive T cells continued for another two grant cycles. Both of us were attracted into administrative positions around the university and we gradually developed different research areas provided within the new environment. Research interests naturally evolve. My own interest in membrane trafficking moved from model systems to Alzheimer’s disease with help from individuals in my immediate environment, especially through Andy Hill’s intellectual input, reagents and contacts and later with Danny Hatters. In Search of Memory by Eric Kandel (2006) provided a wonderful entree into the history of neuroscience. In addition, opportunities arose with industry within Bio21, and I have been fortunate in successfully obtaining a series of ARC Linkage grants with CSL on the cell biology and trafficking of the neonatal FcR receptor and the capacity to extend the half-life of novel therapeutic proteins. The Golgi apparatus also remains a close friend and we are exploring a number of new functions of this organelle that shows its ability to act as a cell sensor, akin to other intracellular organelles.

Great Expectations


Head of DepartmentI agreed, initially reluctantly, to take over as head of

department in 2006 when Mary Jane Gething retired. My period as head for ten years was very busy and very rewarding. It is worth noting for younger scientists that in all our recruitment processes, the department actively sought people who had demonstrated that they are willing and able to collaborate with their peers from day one. It was particularly rewarding to build up the research strength in the department by recruiting and mentoring young/early career lab heads and to witness their well-deserved success with grants and fellowship applications. It was also very satisfying to recruit and support the teaching specialists in the department who now have the same opportunities to advance their careers as the researchers. From the considerable support I received from other staff members, I was able to keep my research group going during this period. I also maintained a full undergraduate teaching load, as I think it essential to be engaged in this core university activity. Teaching enriches and generates research ideas.

Sabbaticals Mini-sabbatical made a lasting impression on me. The

standouts are six months at EMBL, Heidelberg, and three months at the Curie Institute, Paris. EMBL is like a big family and, as the majority of researchers are early career scientists from all over Europe, the network established blossoms for many years. My connection with the Curie also opened up an opportunity to become a member of the Human Program Science Program Fellowship committee, which I served on for four years. My strong advice is to visit places based not only on the specific lab, but also the broader environment and culture.

HolidaysI have always considered holidays to be important and

I made sure that I took some. Research is intense often involving evening and weekend work. Holidays that take you to a different mindset and place are the best, and even a few days can make a difference, such as bush walking in the wilds of Tasmania. Find ways of doing this. When our kids were small, we took long service leave and travelled around Australia with our young children for ten weeks. From Heidelberg at EMBL we drove to a conference in Milan then onwards to southern France. During the period at the Curie we spent six weeks as a family in a small apartment in the Latin Quarter exploring Paris on foot. More recently, I have discovered a hotel specialising in cycling trips on the Adriatic coast of Italy.

FAOBMBAn opportunity arose when the then ASBMB President,

Leann Tilley, invited me to consider the position of ASBMB delegate for the FAOBMB. Australia has been a very active participant in this Asian and Oceanian federation from its foundation nearly 50 years ago. This has unexpectedly taken me into a new world. Delegates from 21 national societies in our region work together to organise meetings, conferences and congresses, and encourage young scientists by various programs and awards. I am now Fellowship Chair of the FAOBMB and work closely with a wonderful group of people who are generous with their time. My involvement has provided opportunities to visit regional countries, including Japan, Philippines, South Korea, China and Pakistan. This year would have been Sri Lanka, if not for COVID-19. It is very impressive to meet young dedicated scientists working in very challenging environments. The funding for programs via the FAOBMB makes a big difference to their career development and networking. There is probably more I could add, especially to encourage involvement in conference organising – maybe for another time.

Great Expectations

The Gleeson lab group in 2020.

FAOBMB Executive at the FAOBMB Conferenceheld in Kuala Lumpur, Malaysia, in 2019.


Australian Beer is CRISPRSpend enough time away from home and you start to miss the simplest of things

After completing my PhD with Professor Charles Bond and Associate Professor Archa Fox at the University of Western Australia in 2016, I relocated to the United States where I have been working as a postdoctoral fellow with Professor Jennifer Doudna at the University of California, Berkeley. By early 2019, I was searching for a conference that would take me back to Australia where I could present my recent work, catch up with family, and get my hands on a good lager! Originally from Western Australia, I was excited to see that the ASBMB 2019 meeting was going to be in Perth, and in Fremantle no less (go the Dockers!). After registering and applying through the ASBMB, I was thrilled when I received the email saying I had been awarded the 2019 ASBMB Boomerang Award. What a great opportunity! With the generous support offered from the ASBMB, I was able to plan a whirlwind trip across Australia, eager to pack in as much as I could while I was home.

In mid-September I flew across the Pacific to Melbourne where in rapid succession I presented my work at Monash University, St Vincent’s Institute and La Trobe University. It was an absolute privilege to have the opportunity to present at each institute. Australia is home to an incredible diversity of scientists and it was great to network with colleagues who offered both great questions and critical feedback. After what was an incredible four days in Melbourne (featuring a solid reintroduction to Australian coffee, food and beer), I skipped across to Sydney where I presented my work at the Victor Chang Cardiac Research Institute. Come AFL Grand Final day, I jumped onto a plane bound for Perth, right on time

to sit down, beer in hand and watch the game with my family. After a few days of catching up, it was time for the ASBMB 2019 meeting in Fremantle.

My postdoctoral research has been focused on the molecular evolution of CRISPR-Cas systems, a constant evolutionary back and forth that has generated a plethora of biotechnologically applicable tools. To my delight, the first day of the ASBMB 2019 meeting featured applications of CRISPR-Cas in cancer, gene discovery, and even drug discovery in fungi! The ASBMB 2019 meeting showcased the mechanistic elegance at the heart of biology but also the raw talent of both Australian and international scientists. It was an incredible honour to present my work amongst such a stellar array of speakers and I cannot thank the ASBMB enough for their support. Beyond the intellectually engaging science, it was a great opportunity to network with colleagues and revisit some old haunts from the PhD days.

Before I knew it, the conference was over, everyone was headed back to work and I made my way back across Australia to San Francisco. It was an amazing trip back home: one that saw a healthy exposure to remarkable science, good times spent with friends and family, and perhaps an unhealthy exposure to the comforts of familiar food and beer. I cannot thank the ASBMB enough for the opportunity and their continued support. I eagerly look forward to my next trip back to Australia!

Gavin Knott is a Research Fellowat Monash University, currently based

at the University of California, Berkeley.

ASBMB Boomerang Award Report

ASBMB President Joel Mackay congratulates Gavin at ASBMB 2019.

Gavin enjoys dinner in Fremantlewith ASBMB 2019 attendees.


Continuing our series of articles on intellectual

property, Anthony Selleck, Patent Attorney, FPA Patent

Attorneys, discusses howadvancesinartificial

intelligence in the medical fieldcanbeprotected.

While the use of artificial intelligence (AI) in medicine has a long history, the last few years have seen an explosion in interest and investment in this field of technology. AI, and in particular, ‘machine learning’, is being applied to develop new products and processes for use in both medical research and clinical practice. Patents are the classic species of intellectual property rights used to protect medical innovations such as new pharmaceuticals, genetic technologies and medical devices. However, when it comes to protecting AI-related innovation through the patent system, certain challenges remain. This article will examine the latest applications of AI in medicine and provide guidance for identifying aspects of AI projects that may be protectable by patents.

AI and machine learningThe term ‘artificial intelligence’ was coined in 1956 to

refer to computer programming techniques that seek to mimic human intelligence. During the 1960s and 1970s, AI progressed into the development of ‘expert systems’, where computers were programmed to simulate the decision-making processes of human experts. Such systems were the first to apply AI to the realm of medicine by designing computer programs that would assist in the process of medical diagnosis.

The 1980s and 1990s saw the development of a new approach known as ‘artificial neural networks’. These are a network of computing units that are connected and controlled in a manner that (supposedly) resembles the neurons in the human brain. Each neuron performs a small computational task (typically matrix multiplication) and communicates its results to other neurons. In contrast to earlier approaches, the logical rules are not ‘manually’ coded into the system. Instead, the artificial neural network derives the rules itself (and thus ‘learns’) from a large dataset that is input to the system.

After a surge of interest, artificial neural networks fell out of favour by the end of the 1990s. However, starting in the early-2010s with some well-publicised advances in artificial neural network-assisted language translation, strong interest in the technology returned. The interest and investment remains very much in place today, no

more so than in the field of medicine. ‘Deep’ networks (that perform ‘deep learning’) are

one of the key technical breakthroughs underlying modern artificial neural networks. In contrast to the flat topology of earlier approaches, deep learning networks are arranged in layers, each of which contains several thousand neurons. The first layer is fed with a large input dataset that contains examples of the phenomenon that the network is to model. In the medical domain, the input dataset could be any form of biomedical data, such as medical images with particular features, symptoms and associated diagnoses, candidate drug compounds and/or genomic data.

The system connects the neurons in the layers to perform a structured sequence of computations that define a model that can be used to make predictions from input data. The robustness of the model is tested by running the input dataset through the neural network and determining how well it performed its task. Any deficiencies in the model are used to rearrange the connection patterns between the neurons and thereby improve the model’s accuracy. Once the model converges to a desired level of accuracy (which may involve many iterations), the artificial neural network is evaluated by processing a new dataset of unseen values. This provides an indication of how the model might perform in the real world when processing data on which it has not been trained.

Protecting AI innovationsWith the increase in the availability of medical imaging,

biomedical, genomic and epidemiological datasets, deep learning techniques are being harnessed to develop solutions across a range of medical domains.

Radiology is a natural application, where artificial neural networks can be readily trained with medical imaging datasets to be able to recognise and essentially diagnose diseases captured in an image. In this regard, machine learning algorithms are increasingly being integrated into the workflow of radiology software to assist clinicians.

More ambitiously, AI is being used in the task of drug discovery. In this application, the artificial neural network is trained with suitable biomedical data in order to:• Identify previously unknown disease mechanisms

and/or pathways; • Identify potential treatments on the basis of the

determined mechanisms;• Generate more predictive hypotheses based on

patient-driven biology and genetic profiles.However, these new approaches beg the question about

what aspects of an AI project are potentially protectable through the patent system. In this regard, it is a cardinal requirement before a patent will be granted that there is a new and non-obvious invention. Inventions involving new algorithms and computer software also tend to be

Artificial Intelligence in Medicine – What is Patentable?


carefully scrutinised for compliance with the requirement of ‘patentable subject matter’. In common with patents for certain classes of diagnostic method, AI patents are sometimes rejected as being directed to a scientific discovery rather than to a human-made invention.

While merely training an artificial neural network on a new dataset is in itself unlikely to constitute a patentable invention, there is still broad scope for securing protection over other aspects of an AI project.

For example, changes made to the mathematical underpinnings of an artificial neural network – such as to improve its performance with particular types of biomedical data – are potentially patentable. Indeed, it was the development of new underlying algorithms (and especially in the field of back-propagation) that drove the breakthroughs in deep learning technologies in the early 2010s.

Another area of potentially patentable technology is the development of artificial neural networks that generate the initial training datasets that are used by other neural networks. This can be particularly important in the investigation of rarer diseases and disease pathways for which definitive datasets may not be available.

Techniques for ‘conditioning’ biomedical data to make it more amenable to serving as training data for an artificial neural network are also potentially patentable. In this regard, mathematical techniques to automatically classify and label digital images, videos, audio or speech signals based on low level features, could form the subject of a patentable invention.

Finally, there is broad scope for patentable invention to arise when AI systems are interfaced with other medical equipment and devices. For example, use of a neural network in a heart-monitoring apparatus, or to drive digital imaging systems, has the potential to be patentable.

AI as an inventorA recent issue that has arisen is whether an AI can make

inventions itself, and thus should be named as such on a patent application. Attempts have already been made to file patent applications in the name of an AI inventor, however these have been rejected by the UK and US patent offices. The UK Intellectual Property Office has also now issued updated guidance to the effect that any patent application which names an AI as the inventor will not be accepted, as the inventor must be ‘a person’.

The European Patent Office has also weighed into the issue by releasing guidance observing that AI systems ‘at present’ have no rights, and that ‘no … law has [yet] been determined which would recognise… an AI… as an inventor’. However, the EPO did not go so far as to say that it would be impossible for any AI to be recognised as an inventor in the future.

ConclusionsIn light of the substantial investment involved in building

and deploying AI in a research or clinical context, careful consideration should be given to protecting as much of the underlying technology as possible. This requires a sharp focus on the innovative aspects of the technology –either in the AI itself or in its integration with other systems and equipment – to ensure that commercially valuable patent rights are sought. In addition, if the technology encompasses new algorithms, to head off an objection that the application is not directed to patentable subject matter, it is important to include extensive disclosure of the practical applications for the new algorithms.

[email protected]

Artificial Intelligence in Medicine – What is Patentable?

Australian Society for Biochemistry and Molecular Biology IncPUBLICATION SCHEDULE FOR AUSTRALIAN BIOCHEMIST, volume 51, 2020

Issue

April 2020 51(1)

August 2020 51(2)

December 2020 51(3)

ASBMB Content

Profiles of medal, award and fellowship winnersNominations for Executive/Council

Nominations for medals, awards and fellowshipsNotice of AGM/proposed constitutional changes

Annual reports/finances

Copy Deadline

Monday 10 February

Monday 8 June

Monday 5 October

Issue Date

Monday 6 April

Monday 3 August

Monday 30 November


Science Teachers’ Association of Victoria – Science Talent Search

Assembly of our future scientists at the 2019 Science Teachers’ Association of Victoria Science Talent Search.

The Victorian branch of the ASBMB continued its Gold Sponsorship of the annual Science Talent Search in October 2019. It was once again held at La Trobe University. This is a much cherished event on the school calendar for budding scientists. Founded in 1952, the event, organised by the Science Teachers’ Association of Victoria, is aimed at:• Encouraging students to consider the serious study

of Sciences by encouraging independent project work amongst science students, providing students the opportunity to communicate their achievements to a wider audience and to enjoy recognition for their efforts and achievements.

• Promoting the direct involvement of students in science and its communication.

• Enabling public recognition of the quality of the work achieved in Science by Victorian students.

The theme for 2019 was ‘Destination Moon: More Missions, More Science’. Students enrolled in Prep through to Year 12 were invited to submit projects in 10 categories: Computer Programs, Games, Science Photography, Posters and Scientific Wall Charts, Working Models, Inventions, Experimental Research, Creative Writing, Video Productions and Class Experimental Research Project. The 3,271 young scientists who entered 2,327 submissions from 165 schools attest to the popularity of the event.

The Victorian Branch of the ASBMB supported the 2019 Science Talent Search with a $1,000 donation, in the form of major and minor bursaries awarded to ten students from primary and high schools in Victoria. These schools included: Camberwell Girls Grammar School, Genazzano FCJ College, Glen Eira College, Glendal Primary School, Paynesville Primary School, Presbyterian Ladies’ College, Sirius College and Strathcona Baptist Girls Grammar School. Project titles included ‘Battle against the bacteria’, ‘The effect of storage time on protein contents of Australian chicken eggs’, ‘What is the most effective method of removing

pesticide off kale?’ and ‘Maximising the amount of protein in yoghurt using different milk samples’. Perhaps some of us can tap into these young minds for inspiration for our next round of NHMRC Ideas grants submissions?

One of the most satisfying aspects serving as Victorian State Representative is receiving hand-written and sometimes typed letters of appreciation from our young award recipients. Many express a desire to pursue a future career in science and research. Their sincerity and sense of appreciation in their meaningful messages proves that our support of such events should be continued for many years to come.

Erinna Lee ASBMB Victorian State Representative

www.sciencevictoria.com.au/sts

An award-winning student projectthat depicts how the pancreas works.


Australia Day Honour for ASBMB Member

Emeritus Professor Mitchell Guss was made an Officer of the Order of Australia (AO) for distinguished service to education and scientific research in the field of molecular bioscience, and to professional organisations.

Professor Guss’ research is based on the determination of molecular structure, principally by the technique of X-ray diffraction, and the relationship of the structures to chemical or biochemical function.

It was his first Chemistry lecture as an undergraduate at the University of Sydney that drew Mitchell into the world of protein structure, long before it was possible to apply the technique of crystallography to proteins in Australia. In that lecture, Professor Hans Freeman, later Guss’s Honours and PhD supervisor, drew attention to the Nobel Prizes that had been awarded a few months earlier to Perutz and Kendrew for protein structure and to Watson, Crick and Wilkins for the structure of DNA.

After five years as a postdoctoral fellow in the UK and the USA, he returned to Australia to rejoin Freeman’s group, then attempting the first protein crystal structure in Australia. With Peter Colman and others, this effort eventually resulted in the structure of plastocyanin, a ‘blue’ copper protein, providing an explanation for the extraordinary spectroscopic and redox properties of this family of proteins. Later work on another ‘blue’ copper

protein provided the first use of multi-wavelength anomalous diffraction (MAD) phasing to solve a de novo structure.

On Hans’ formal retirement in 1994, Guss moved the laboratory from the School of Chemistry to the Department of Biochemistry. Subsequent collaborations both within the University of Sydney, elsewhere in Australia and internationally, resulted in many new structures mostly of metallo-enzymes, including sulfatase, amine oxidase and proline aminopeptidase.

Professor Guss has been an Editor of Acta Crystallographica and the Journal of Molecular Biology. He has served as President of the Society of Crystallographers in Australia and New Zealand and of the Asian Crystallographic Association. He was a member of the International Union of Crystallography executive for six years. His pioneering use of synchrotron radiation sources led to appointments on scientific advisory committees for the NIH and the Australian Synchrotron.

He notes with thanks that his publications include more than 200 co-authors who as students and collaborators have made the major contributions to the science that have enabled his award.


Robert Gerard (Gerry) Wake FAA 1933–2020Gerry Wake made basic

research the top priority during his career (1953-2000). Research-led teaching meant that undergraduate students could be taught right up to the cutting edge of the discipline.

When I arrived as a Lecturer in the Department of Biochemistry at the University of Sydney in 1986, Gerry and Philip Kuchel were alternating

Heads of Department on a 2-year cycle. It was clear to me that they were the ‘dynamic duo’ in research and led from the front, gaining excellent research students and substantial research grants. I was amongst the first of a new wave of academic staff that revitalised the Department; we were selected with research as the top priority under this dynamic leadership. The result was that over the period 1986–2010, our Department developed many powerful research programs. In more recent times, much of this research talent has been taken up by the Charles Perkins Centre.

Gerry undertook his BSc studies at the University of Sydney, completing his Honours project in 1953 on protein denaturation under the supervision of Dr Hugh McKenzie of the CSIRO. Gerry continued to his MSc then PhD in protein chemistry, under McKenzie’s supervision, working on the caseins of milk and the stabilisation of casein micelles. McKenzie imparted the discipline characteristic of the physical sciences and had a superbly equipped laboratory that included an analytical ultracentrifuge. Gerry completed his PhD in 1958 and moved to the University of Wisconsin at Madison to work with Robert L (Buzz) Baldwin.

Buzz was only five years older than Gerry and already well known for his studies on ultracentrifugation. He was influential in developing Gerry’s approach to research and they remained lifelong friends. When Gerry and his wife Aileen arrived in Madison, the weather was extremely cold. Buzz was not there but had left a coat and scarf, one of many kindnesses extended to them during their two and a half years in the USA. After 6 months, Gerry moved with Buzz to Stanford University. Wake and Baldwin published papers together both on caseins and DNA replication. At Stanford, Arthur Kornberg had just published his pioneering work on the DNA polymerase from Escherichia coli for which he later received the Nobel Prize. The central aim at Stanford was always to understand biological systems at a molecular level, Gerry shared this priority and always advocated basic research. During the two years at Stanford, Gerry took up work on DNA replication that became the field of research in which he excelled for the

remainder of his career. On his way back to Australia, Gerry spent six months in Oxford investigating the reactivity of disulphide bonds in proteins with Rupert Cecil. He and Aileen enjoyed Oxford so much that Gerry returned for a sabbatical in 1978 with Professor Joel Mandelstam.

Gerry arrived back at the University of Sydney in late 1961. He continued with research on the biological activity of κ-casein. Gerry and Buzz Baldwin had developed a procedure for the analysis of the mixture of caseins present in milk micelles by starch–urea gel electrophoresis, revealing a series of discrete bands and one enigmatic smear representing κ-casein. Interestingly, κ-casein was behaving as an extremely complex mixture of species defying conventional analysis. Gerry had the insight to treat the κ-casein complex with disulphide bond-cleaving reagents to greatly simplify the electrophoretic pattern, revealing a finite number of protein species, which in different combinations were giving rise to the great complexity of the original pattern (upper image on next page). The purification of the individual κ-casein components provided the basis of the project for his first PhD student Tony Mackinlay. Further characterisation by his second PhD student, Ron Hill, including amino acid analysis of different regions of κ-casein molecules, provided one of the first recognitions of partitioning of polar and non-polar amino acids within a protein. κ-Casein was functioning as an amphiphile: analytical ultracentrifugation showed that the hydrophobic N-terminal region of the molecule could interact with the other caseins whilst the hydrophilic end (with one residue in three either Ser or Thr), does not but rather provides a solvated water coat. Rennin splits κ-casein once between the hydrophobic and hydrophilic regions destabilising casein micelles leading to curds and whey.

In Memoriam

Gerry Wake.

Gerry and Buzz Baldwin.Photo: Ross Inman, Stanford University, 1961.


Gerry receives the 25-year long service medal from Sir Hermann Black, Chancellor, University of Sydney, 1984.

Gerry’s subsequent research was focused on DNA synthesis in the bacterium, Bacillus subtilis, the movement of replication forks on the circular chromosomal DNA, and their arrest at completion of a cycle of DNA replication. In 1971, Gerry made a major discovery about replication of DNA in bacteria. Using a microscope and the technique of autoradiography, he determined the topology of DNA within a replicating multi-forked bacterial chromosome. He found that DNA synthesis occurred in both directions from a unique origin, rather than in one direction, as had been generally accepted (lower image, opposite). For this and other major contributions, Gerry was elected as a Fellow of the Australian Academy of Science in 1985. His subsequent research focused on his dual fascination with the termination of chromosome replication and cell division in B. subtilis. Tony Weiss, who was a PhD student in Gerry’s lab and is now the McCaughey Chair in Biochemistry at Sydney University (formerly Gerry’s chair) fondly recalls the joy of being supervised by Gerry, and the excitement of identifying the replication terminus terC on the bacterial chromosome. Gerry continued to lead this new field by characterising the roles and structure of the protein RTP (replication termination protein) that bound to terC. His 1995 review with long-term friend and colleague Jeff Errington FRS entitled ‘Chromosome partitioning in bacteria’ illuminated our fundamental understanding of the field. Gerry’s pioneering research aided the construction of the genetic and restriction site maps of B. subtilis which, in turn, guided the complete sequencing (by others) of the genome of B. subtilis, a forerunner to thousands of sequenced bacterial genomes. It has also contributed to our analysis of DNA replication in humans.

In Memoriam

The enigmatic continuum of molecular species presented by κ-casein on starch-urea gel electrophoresis.a. Analysis of κ-casein into a finite series of bands following reduction of disulphide bonds by mercaptoethanol and alkylation under denaturing conditions employing b. 3 M guanidine hydrochlorideor c. 8 M urea.Reproduced from Hill RJ (1965) Studies on the action of rennin on κ-casein. MSc thesis. University of Sydney.

Gerry’s influential autoradiograph of symmetrically reinitiated chromosomes demonstrates bidirectional replication. Only the replicated DNA strands are radioactively labelled (unbroken lines in the scheme) allowing only the replicated double-helical chromosomal regions to be visible in the autoradiograph.Reproduced with permission from Elsevier: Wake RG (1972) J Mol Biol 68:501–509.


One of Gerry’s greatest academic legacies lives on through the graduate students he trained in the art of scientific research. On arrival in his laboratory each student had some very general notions of the nature of research. Gerry taught by example that behind his beautiful and outstandingly elegant research there lay a concealed art: organisation, planning and an uncanny ability to look at complex phenomena to see underlying simpler mechanisms upon which one could focus investigations. The approaches he imparted led his students on to highly successful careers in research and teaching, many at professorial level and including directorships of research institutes.

One year before Gerry’s retirement in 2000, while I was Head of School, I commissioned Judy Cassab (twice an Archibald Prize winner) to paint Gerry’s portrait. Gerry may have been initially a little doubtful, but the portrait was completed with six sittings at Judy’s house and was a wonderful experience for Gerry. They became good friends and the portrait displays many of Gerry’s attributes, a keen mind with penetrating eyes, long fingers useful for lab work, and the microscope with which he made his major discovery relating to bidirectional DNA replication. Gerry’s portrait hangs prominently in the Molecular Bioscience Building at the University of Sydney.

Gerry gave his time generously to the Australian scientific community. He served on Council of the Australian Academy of Science (1990–1993) and as Vice-President (1991–1992), as well as on the National Committee for Biochemistry and the Boden Research Conferences selection committee. He was well known in ARC grant circles in the 1980s for his travel to different cities to interview applicants face to face. Gerry was Treasurer of the Australian Biochemical Society (1970–1973) and served as President (1984–1986).

After his retirement, Gerry continued to play tennis regularly at Sydney University with a notable group of scientific colleagues. In later years Gerry developed Parkinson’s Disease, which he faced with great courage. He was a very fine man, a loving husband to Aileen, a devoted father to Rachel and Simon, father-in-law and grandfather. The extraordinary collection of scientists at Gerry’s funeral and the long list of former students and colleagues who provided condolences by email attest to his inspirational legacy. He was father and grandfather of a large scientific community. His human and scientific legacies will live on.

Richard Christopherson with the assistance ofRon Hill, Tony Weiss and Philip Kuchel

In Memoriam

Three generations of the Wake family, 2017.

Gerry with the microscope he used to demonstrate bidirectional replication of the Bacilis subtilis

chromosome. Portrait by Judy Cassab, 1999.


For further information visit

FA O B M B 2 0 2 1 . O R G

We are excited to welcome you to

Christchurch, New Zealand for the

16th Congress of the Federation of

Asian and Oceanian Biochemists

and Molecular Biologists.

This will also be ASBMB’s annual

meeting in 2021.

Peak Bodies

Hosts

22–25 NOVEMBER 2021


For further information visit

FA O B M B 2 0 2 1 . O R G

We are excited to welcome you to

Christchurch, New Zealand for the

16th Congress of the Federation of

Asian and Oceanian Biochemists

and Molecular Biologists.

This will also be ASBMB’s annual

meeting in 2021.

Peak Bodies

Hosts

22–25 NOVEMBER 2021

DisclaimerThe Australian Biochemist is published by the Australian Society for Biochemistry and Molecular Biology Inc. The opinions expressed in this magazine do not necessarily represent the views of the Australian Society for Biochemistry and Molecular Biology Inc.

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Laboratories Credit Union (LCU) was founded in 1954 by a group of CSIRO employees who formed the credit union with the aim of helping staff to gain access to finance. Back in those days the loans were generally of small value and were for things like the purchase of white goods. Over the years the credit union has grown and has been offering home loans since the late 1980s and now provides a full range of banking products to all members.

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Abcam: Expanding PortfolioAbcam has had a busy year expanding

its cell engineering capabilities through an asset purchase of Applied StemCell’s gene editing platform and oncology product portfolio. Abcam also acquired EdiGene’s knock-out cell lines and lysates portfolio. This has enabled Abcam to launch new CRISPR-Cas9 knock-out cell lines and cell lysates for target identification, validation and pathway discovery.

Further, Abcam completed the acquisition of Expedeon’s proteomics and immunology business, enhancing its conjugation capability. Abcam and SomaServe announced comprehensive partnership to realise the potential of PolyNaut® ‘bionic’ nanoparticles for delivery to live cells. Abcam and BrickBio announced a partnership to incorporate conjugation-ready sites into recombinant antibodies across Abcam’s portfolio. Further information is available at abcam.com.

Nano-Boosters and Nano-Labels

ChromoTek’s Nano-Boosters and Nano-Labels are fluorescent probes. They consist of very small recombinant antibody domains, also called Nanobodies or VHHs. These single-domain alpaca antibody fragments are covalently coupled to fluorescent dyes.

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https://www.atascientific.com.au/products/celena-x-high-content-auto-cell-imaging-system/



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ASBMB Council 2020

TREASURERProfessor Marc Kvansakul Department of Biochemistry and GeneticsLa Trobe Institute for Molecular Science La Trobe UniversityBUNDOORA VIC 3086Ph (03) 9479 2263Email: [email protected]

PRESIDENTProfessor Joel MackaySchool of Life and Environmental SciencesUniversity of SydneySYDNEY NSW 2006Ph (02) 9351 3906Email: [email protected]

SECRETARY FOR SUSTAINING MEMBERSSally Jayc/- ASBMB National OfficePO Box 2331KENT TOWN SA 5071Ph (08) 8362 0009Email: [email protected]

EDUCATION REPRESENTATIVEDr Nirma SamarawickremaDepartment of Biochemistry and Molecular BiologyMonash UniversityCLAYTON VIC 3800Ph (03) 9902 0295Email: [email protected]

EDITOR and CHAIR OF COMMUNICATIONS Dr Tatiana Soares da CostaDepartment of Biochemistry and GeneticsLa Trobe Institute for Molecular Science La Trobe UniversityBUNDOORA VIC 3086Ph (03) 9479 2227Email: [email protected]

FAOBMB REPRESENTATIVEAssociate Professor Terrence PivaSchool of Medical SciencesRMIT University, PO Box 71BUNDOORA VIC 3083Ph (03) 9925 6503Email: [email protected]

SECRETARYProfessor Briony ForbesMedicinal BiochemistryFlinders UniversityBEDFORD PARK SA 5042Ph (08) 8204 4221Email: [email protected]

PRESIDENT ELECTProfessor Jacqui MatthewsSchool of Life and Environmental SciencesUniversity of SydneySYDNEY NSW 2006Ph (02) 9351 6025 Email: [email protected]

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COUNCIL FOR2020PRESIDENTProfessor Joel MackaySchool of Life and Environmental SciencesUniversity of SydneySYDNEY NSW 2006Ph (02) 9351 3906Email: [email protected]

PRESIDENT ELECTProfessor Jacqui MatthewsSchool of Life and Environmental SciencesUniversity of SydneySYDNEY NSW 2006Ph (02) 9351 6025Email: [email protected]

TREASURERProfessor Marc Kvansakul Department of Biochemistry and GeneticsLa Trobe Institute for Molecular Science La Trobe UniversityBUNDOORA VIC 3086Ph (03) 9479 2263Email: [email protected]

SECRETARYProfessor Briony ForbesMedicinal BiochemistryFlinders UniversityBEDFORD PARK SA 5042Ph (08) 8204 4221Email: [email protected]

EDITOR and CHAIR OF COMMUNICATIONSDr Tatiana Soares da CostaDepartment of Biochemistry and GeneticsLa Trobe Institute for Molecular Science La Trobe UniversityBUNDOORA VIC 3086Ph (03) 9479 2227Email: [email protected]

EDUCATION REPRESENTATIVEDr Nirma SamarawickremaDepartment of Biochemistry and Molecular BiologyMonash UniversityCLAYTON VIC 3800Ph (03) 9902 0295Email: [email protected]

FAOBMB REPRESENTATIVEAssociate Professor Terrence PivaSchool of Medical SciencesRMIT University, PO Box 71BUNDOORA VIC 3083Ph (03) 9925 6503Email: [email protected]

SECRETARY FOR SUSTAINING MEMBERSSally Jayc/- ASBMB National OfficePO Box 2331KENT TOWN SA 5071Ph (08) 8362 0009Email: [email protected]

STATE REPRESENTATIVESAUSTRALIAN CAPITAL TERRITORYDr Matthew JohnsonResearch School of BiologyAustralian National UniversityACTON ACT 2601Ph (02) 6127 0049Email: [email protected]

NEW SOUTH WALESDr Kate Quinlan School of Biotechnology and Biomolecular SciencesUniversity of New South WalesSYDNEY 2052 NSWPh (02) 9385 8586Email: [email protected]

QUEENSLANDDrBenjaminSchulzSchool of Chemistry & Molecular BiosciencesUniversity of QueenslandST LUCIA QLD 4072Ph (07) 3365 4875Email: [email protected]

SOUTH AUSTRALIADr Melissa PitmanCentre for Cancer BiologySA Pathology & University of South AustraliaADELAIDE SA 5001Ph (08) 8302 7892Email: [email protected]

TASMANIADr Kate Brettingham-MooreSchool of MedicineUniversity of TasmaniaHOBART TAS 7008Ph (03) 6226 4609Email: [email protected]

VICTORIADr Erinna LeeOlivia Newton-John Cancer Research Institute145 Studley RdHEIDELBERG VIC 3084Ph (03) 9496 5726Email: [email protected]

WESTERN AUSTRALIADr Monika MurchaARC Centre of Excellence in Plant Energy BiologyUniversity of Western AustraliaCRAWLEY WA 6009Ph (08) 6488 1749Email: [email protected]

ASBMB NATIONAL OFFICEPO Box 2331KENT TOWN SA 5071Ph (08) 8362 0009Fax (08) 8362 0009Email: [email protected]://www.asbmb.org.au

SPECIAL INTEREST GROUPSADELAIDE PROTEIN GROUPChair: Erin BrazelUniversity of AdelaideADELAIDE SA 5005Ph (08) 8313 8259Email: [email protected]

AUSTRALIAN YEAST GROUPChair: Dr Alan MunnGriffith University Gold CoastSOUTHPORT QLD 4222Ph (07) 5552 9307Email: [email protected]

BIOCHEMICAL EDUCATIONChair: Dr Nirma SamarawickremaMonash UniversityCLAYTON VIC 3800Ph (03) 9902 0295Email: [email protected]

CELL ARCHITECTUREChair: Associate Professor Thomas FathDementia Research CentreMacquarie UniversityNORTH RYDE NSW 2109Email: [email protected]

MELBOURNE PROTEIN GROUPPresident:DrMichaelGriffinBiochemistry and Molecular BiologyBio21 Institute, University of MelbournePARKVILLE VIC 3010Ph (03) 9035 4233Email: [email protected]

METABOLISM AND MOLECULARMEDICINE GROUPChair: Dr Nigel TurnerUNSW SydneyKENSINGTON NSW 2052Ph (02) 9385 2548Email: [email protected]

PERTH PROTEIN GROUPChair: Associate Professor Joshua MylneUniversity of Western AustraliaPERTH WA 6009Ph (08) 6488 4415Email: [email protected]

QUEENSLAND PROTEIN GROUPChair: Dr Brett CollinsInstitute for Molecular Bioscience, UQST LUCIA QLD 4072Ph (07) 3346 2043Email: [email protected]

RNA NETWORK AUSTRALASIAChair: Dr Archa FoxHarry Perkins Institute of Medical ResearchNEDLANDS WA 6009Ph (08) 6151 0762Email: [email protected]

SYDNEY PROTEIN GROUPPresident: Dr Tara ChristieSchool of Life and Environmental SciencesUniversity of SydneySYDNEY NSW 2006Ph (02) 9685 9926Email: [email protected]

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