My research focuses on the molecular interactions that take place in human cells in human and viral RNA biology, innate immunity and cellular signalling.

The laboratory, run jointly with A/Prof Matthew Wilce, aims to better understand molecular recognition by determining the overall shapes, as well as the precise three-dimensional structures of macromolecular complexes and by testing their affinity and specificity using biophysical techniques. We investigate several molecular systems involved in RNA biology, innate immunity and cancer cell progression. These include the study of proteins which bind to mRNA and regulate translation, proteins which recognise RNA in innate immunity and the development of peptides which inhibit cancer cell proliferation and migration.

Current Research Projects

Protein-RNA interactions in antiviral cellular defence and inflammation

Protein-RNA interactions are integral to cellular biology – both in normal cellular function and also in cells subject to the stresses of viral invasion. Proteins are responsible for the detection of viral RNA, and initiation of the innate immune response. Proteins direct post-transcriptional regulation of cytokines produced as a result of cellular stress, and are responsible for preventing their over-expression. In some cases, cellular proteins that normally function in translational control are hijacked by viral RNA as part of the viral mechanism of replication in the cell. Underlying each of these types molecular events are intricate and specialised molecular interactions. Their understanding would greatly advance our knowledge of antiviral cellular defence and potentially lead to new means to combat virus-related disease and inflammatory disorders.

Our lab has specialised in the study of protein-RNA interactions, using biophysical and structural tools to better understand the basis for their affinity, specificity and conformational consequences underlying their mechanism of action. Our objective is to delineate specific protein-RNA systems relevant to antiviral cellular defence.

I completed a B. Sc (Hons) degree at Monash University, specialising in novel peptide chemistries at honours level. In 1994 I graduated with a Ph.D. in Medicinal Chemistry from the Victorian College of Pharmacy (now MIPS, Monash University) in the field of NMR structural and dynamics studies of peptides and proteins. I then took up a position at Queensland University in the Centre for Drug Design and Development with Professor David Craik, synthesising proteins using peptide and novel linkage chemistries. I then spent several years at the University of Sydney with Professor Glenn King, extending my expertise to include molecular biological and protein expression and purification techniques as well as 3D heteronuclear NMR spectroscopy and analytical ultracentrifugation. Here I began to develop an interest in structural and dynamic studies of novel cancer targets as well as the use of peptides for transporting bioactive compounds across cell walls. I also embarked on structural studies of a protein:DNA complex involved in replication fork arrest for which I was awarded an ARC Postdoctoral Fellowship. In 1999 I established my own laboratory as a joint member of Biochemistry and Chemistry at the Department at the University of Western Australia, where I extended my research into the field of structural and dynamic studies of protein-RNA interactions involved in mRNA stabilization in collaboration with partner, Prof Matthew Wilce. In 2001 I was awarded an ARC Fellowship to pursue molecular interactions studies, and have added surface plasmon resonance and isothermal titration calorimetry to the repertoire of biophysical techniques that underpins the work. In 2005 I moved with Matthew Wilce to Monash University to establish labs in the dynamic Department of Biochemistry and Molecular Biology. I was appointed as a Senior lecturer in 2007 and promoted to Associate Professor in 2010. I now engage in both teaching and research in the macromolecular sciences.

I currently teach into the following units:

BMS1011, BCH3031, BMS3031, BMS2062, BCH3052