Colin Ward


Walter and Eliza Hall Medical Research Institute

Colin WardColin Ward is a Fellow of the Australian Academy of Technical Sciences and Engineering and the Australian Institute of Agricultural Science. He is a former Assistant Chief and Deputy Chief of the CSIRO Divisions of Protein Chemistry and Biomolecular Engineering. Colin joined WEHI as a Research Fellow in 2007.

He completed his BSc (1964) and PhD (1967) at the University of New South Wales and was the first student at UNSW to win both a University Medal and a University Blue (Rugby Union). In his postdoctoral work at the University of Massachusetts, Colin elucidated the pathways involved in lipid metabolism during embryonic development of Ascaris lumbricoides and established that these parasites employed a glyoxylate cycle to convert fatty acids into glycogen in preparation for the anaerobic metabolism they would employ once ingested by their host.

He joined the CSIRO Division of Protein Chemistry in 1970 to isolate and characterise more than 29 proteolytic enzymes present in Tineola bisselliella larvae. In 1973, he initiated the influenza virus research in the division. His data on the amino acid sequences of both the haemagglutinin and neuraminidase provided the framework for studies of antigenic variation by nucleic acid sequencing, monoclonal antibody escape mutant selection and X-ray crystallography. A highlight was his prediction, based on sequence analyses, that the haemagglutinin trimers consisted of a coiled-coil, two years before its three-dimensional structure was determined.

From 1985-1992, he attained an international reputation for his work on the structure and variation of plant potyviruses that led to a successful taxonomy of this largest and most complex group of plant viruses. The studies on potyvirus serology and particle assembly led to the production of virus-resistant plants expressing mouse monoclonal antibodies and to a novel application in the field of vaccine technology using the self-assembly properties of the plant virus coat protein.

Since 1990, his research has focussed on the structure and function of the insulin and EGF receptor families. To date, his group is the only one to have obtained high-resolution data for the extracellular ligand-binding region of any member of the insulin receptor family. Highlights include the publication of the structure of the first three domains of IGF-1R in Nature in 1998, of the insulin receptor in PNAS in 2006 and of the whole insulin receptor ectodomain dimer in complex with four Fabs in Nature in 2006.

His group teamed up with Professor Antony Burgess’ group at the Ludwig Institute for Cancer Research and solved the structure of the 2:2 EGFR complex with TGFα and the structure of ErbB2 revealing how the EGFR can form both homodimers and heterodimers with ErbB2.