Walter and Eliza Hall Institute researcher Professor Peter Colman has been elected a fellow of the Royal Society, the UK’s national academy promoting excellence in science.

Professor Colman was the only Australian to be elected a fellow in 2014, and was one of 50 fellows elected this year. The Royal Society announces new fellows each year from the UK and Commonwealth who have made significant contributions in science, engineering and technology. New fellows are elected on the basis of their scientific achievements by existing fellows of the society.

Professor Colman’s interest in the molecular warfare between viruses and their hosts led him to determine the three-dimensional structure of the influenza virus protein neuraminidase in 1983, while at CSIRO. A major result of this work was his discovery of an unchanging part of the neuraminidase protein on the surface of all influenza viruses, suggesting a potential target for anti-influenza drugs.

He led a team of researchers who discovered the anti-influenza drug zanamivir, marketed as Relenza, the first in a then new class of drugs for treating and preventing influenza. The so-called ‘neuraminidase inhibitors’ have been stockpiled by governments around the world as part of the planning for future influenza pandemics that is coordinated by the World Health Organization.

Professor Colman said it was a special honour to be among four crystallographers elected to the Royal Society in the International Year of Crystallography. “I was very fortunate to have a remarkable mentor in the physics department at the University of Adelaide who inspired me to investigate the structure of biological matter by X-ray crystallography,” Professor Colman said. “The influenza work flourished in an environment that encouraged investigator-driven research and allowed me to follow my own scientific instincts. I have enjoyed the unwavering support of my family and my colleagues, all of whom share in this honour.”

Professor Colman’s recent work at the institute is focused on molecules involved in the programmed cell death pathway (also called apoptosis), solving their three-dimensional structures by X-ray crystallography and visualising their interactions with partner molecules that determine whether a cell lives or dies. Understanding the structure of these proteins at an atomic level is essential for drug discovery and development. Targeting specific molecules in the cell death pathway is being pursued as a way of treating a number of diseases including cancers, inflammatory and immune disorders and neurodegenerative diseases.

Institute director Professor Doug Hilton said Professor Colman had made significant contributions to understanding proteins and their structure throughout his career.

“Peter’s research to determine the structures of key viral and cellular proteins has already led to the development of successful drugs for treating disease, which is a great achievement for any scientist,” Professor Hilton said. “In addition to his scientific success, Peter was instrumental to establishing the institute’s structural biology program, which also saw the first integration of medicinal chemists into our institute. It is wonderful to see him honoured by the Royal Society for his accomplishments.”

Professor Colman has received many awards for his research, including the inaugural CSIRO Medal for Research Achievement (1985), the Australian Academy of Science’s Burnet Medal (1995), the Australia Prize (1996, now called the Prime Minister’s Prize for Science), the Australian Government Centenary Medal (2001), the Australian Institute of Policy & Science’s Florey Medal (2004), the Victoria Prize (2008) and the inaugural Bragg Medal of the Society of Crystallographers in Australia and New Zealand (2012).

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Liz Williams
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