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Dr Andrew Brooks is the Group Leader of the Cytokine Receptor Signalling Group at the University of Queensland Diamantina Institute (UQ DI) within the Translational Research Institute. Andrew completed his Honours research on Flaviviruses in 1996 at the Department of Microbiology and Immunology at James Cook University and then moved to the Department of Biochemistry to study Dengue Virus where he completed his PhD in 2002. He then moved to St Jude Children’s Research Hospital in Memphis, TN, USA where he researched the role of Epstein-Barr Virus in B-cell lymphomagenesis. He then joined the research group headed by Prof Michael Waters at the Institute for Molecular Bioscience, UQ in 2006 and subsequently began his independent research group at UQ DI in 2014. Andrew’s research interests are in cytokine receptors, cell signalling, oncogenesis, and immunology. His current research focus is on the molecular mechanisms of class I cytokine receptor activation including the growth hormone receptor (GHR), thrombopoietin receptor (TpoR/MPL), IL-7 receptor, and IL-6 receptor (IL-6R). In addition, he is investigating the regulation of inflammation by HLA-G. His research has led to publications in journals including Science, Blood, Hepatology, Oncogene, Nature Cell Biology, and PNAS. He has been the secured of over $12 million in research and commercialisation funding from sources including NHMRC, ARC, Innovation Connections, and Merck. He has a number of national and international collaborations, a scientific founder of a start-up company, and is an Editorial Board member for the Journal Cancers and Human Cell. He was previously a committee member of Australian Early-Mid Career Researchers Forum (AEMCRF) launched by the Australian Academy of Science.

The molecular evolution of cytochrome P450 Enzymes: biological catalysts of unprecedented versatility.

Cytochrome P450 enzymes (CYPs, P450s) especially those responsible for drug metabolism in humans, are the unifying theme of the research in our lab. These fascinating enzymes are catalysts of exceptional versatility, and functional diversity. In humans they are principally responsible for the clearance of a practically unlimited variety of chemicals from the body, but are also critical in many important physiological processes. In other organisms (plants, animals, bacteria, fungi, almost everything!) they carry out an unprecedented range of functions, such as defense, chemical communication, neural development and even pigmentation. P450s are involved in the biosynthesis of an unequalled range of potent, biologically active natural products in microbes, plants and animals, including many antibiotics, plant and animal hormones, signalling molecules, toxins, flavours and fragrances. We are studying how P450s have evolved to deal with novel substrates by reconstructing ancestral precursors and evolutionary pathways, to answer such questions as how did the koala evolve to live on eucalyptus leaves, a toxic diet for most mammals.

The capabilities of P450s are only just coming to be fully recognized and structural studies on P450s should yield critical insights into how enzyme structure determines function. For example, recently we discovered that P450s are present within cells in the Fe(II) form, a finding that has led to a radical revision of the dogma concerning the P450 catalytic cycle, and has implications for the control of uncoupling of P450 activity in cells. Importantly, the biotechnological potential of P450s remains yet to be exploited. All of the specific research themes detailed below take advantage of our recognized expertise in the expression of recombinant human cytochrome P450 enzymes in bacteria. Our group is interested in finding out how P450s work and how they can be made to work better.

Artificial evolution of P450s for drug development and bioremediation: a way of exploring the sequence space and catalytic potential of P450s. The demonstrated catalytic diversity of P450 enzymes makes them the ideal starting material for engineering sophisticated chemical reagents to catalyse difficult chemical transformations. We are using artificial (or directed) evolution to engineer enzymes that are more efficient, robust and specialized than naturally occurring enzymes with the aim of selecting for properties that are commercially useful in the areas of drug discovery and development and bioremediation of pollutants in the environment. The approach we are using also allows us to explore the essential sequence and structural features that underpin all ~12000 known P450s so as to determine how they work.

Synthetic biology of enzymes for clean, green, solar-powered chemistry in drug development, bioremediation and biosensors. We have identified ancestral enzymes that are extremely thermostable compared to their modern counterparts, making them potentially very useful in industry, since they can withstand long incubations at elevated temperatures. They can be used as ‘off the shelf’ reagents to catalyse useful chemistry, such as in in drug discovery and development, fine chemicals synthesis, and cleaning up the environment. Working with drug companies, we are exploring how they can be best deployed in chemical processes and what structural features make them efficient, robust and specialized. We are also immobilizing P450s in virus-like-particles as ‘designer’ reagents that can be recovered from reactions and reused. To make such processes cheaper and more sustainable, we are using photosynthesis to power P450 reactions for clean, green biocatalysis in microalgae.

Biosketch:

After graduating from UQ with first class Honours in Biochemistry, Elizabeth took up a Royal Commission for the Exhibition of 1851 Overseas Scholarship to pursue doctoral work at Oxford University then undertook postdoctoral work at the Center in Molecular Toxicology and Department of Biochemistry at Vanderbilt University School of Medicine with Prof. F.P. Guengerich. She returned to UQ in 1993 to take up a position in Pharmacology and joined the School of Chemistry and Molecular Biosciences in 2009 as a Professor of Biochemistry.

A/Prof Landsberg's undergraudate and Honours studies, majoring in Chemistry, were completed at Central Queensland University and the CSIRO (JM Rendel laboratories) before he moved to the University of Queensland to study a PhD in Biochemistry (awarded 2003). He then moved to a postdoctoral position at the Institute for Molecular Bioscience, spending time as a Visiting Scientist at Harvard Medical School (2008) and securing promotion to Senior Research Officer upon his return to IMB in 2009. He additioanlly spent time as a Visiting Scientist at the Victor Chang Cardiac Research Institute in 2010 and 2011.

In 2016, he joined UQ's School of Chemistry and Molecular Biosciences as a Group Leader in Cryo-EM and Macromolecular Structure and Senior Lecturer in Biochemistry and Biophysics, where he was promoted to Associate Professor in 2019. He has secured >$13.5M in competitive research funding since 2012, including major grants from the Australian Research Council and National Health and Medical Research Council. He his research has been presented at over 70 national and international conferences and research institutions.

Professor Mobli is a structural biologist and a group leader at the University of Queensland's Australian Institute for Bioengineering and Nanotechnology (AIBN). He is well known internationally for his contributions to the basic theory of multidimensional nuclear magnetic resonance and its applications to resolving the molecular structure of peptides and proteins, as well as studying their physiochemical properties and function. Mehdi's contributions to the field has been recognised by being appointed an Executive Editor of the AMPERE society's journal "Magnetic Resonance", and to the advisory board of the international Biological Magnetic Resonance Data Bank (BMRB) as well as serving on the board of directors of the Australia and New Zealand Society for Magnetic Resonance (ANZMAG). He is a former ARC Future Fellow and recipient of the ASBMB MERCK medal, the Australia Peptide Society's Tregear Award, the ANZMAG Sir Paul Callaghan medal and the Lorne Proteins Young Investigator Award (now Robin Anders Award).

Prof. Mobli's research group focuses on characterising the structure and function of receptors involved in neuronal signalling, with a particular focus on developing new approaches for the discovery and characterisation of modulators of these receptors through innovations in bioinformatics, biochemistry and and biophysics. This work has led to publication of more than 100 research articles attracting over 6,000 citations.