What am I looking at?
The Neuraminidase structure is currently under construction in the UK. Soon we’ll be posting details about its progress. It’s due to arrive at the Shine Dome at the Australian Academy of Science in Canberra later this year.
Why is this crystal structure important?
Swine flu, bird flu, and ‘man’ flu are all caused by the influenza virus. The flu virus is continually changing. What we do know is that there are two molecules, hemagglutinin and neuraminidase, that sit on the surface of the virus and are critical for infection.
Hemagglutinin is responsible for binding to the cells in our body, so that the virus can then inject its viral genome into our cells. Neuraminidase helps to disengage the virus from our cells. The enzyme clips off the chains that anchor the virus to the cell. By blocking the action of neuraminidase, we can stop viral release and spread, and so it has been an important target for flu drugs.
What’s going on in Australia with this material?
The structure of influenza virus A/Tokyo/3/67 neuraminidase was solved in 1991 by two Australian scientists - Peter Malcolm Colman and Joseph Varghese.
Since then the structures of many other varieties of flu neuraminidase have been solved, including the swine flu neuraminidase.
In 1989, scientists at the CSIRO, led by Peter Malcolm Colman and Joseph Varghese, in collaboration with the Victorian College of Pharmacy, Monash University, and Glaxo in the UK, developed the first neuraminidase inhibitor - Zanamivir, which is marketed as Relenza. Its discovery relied heavily on the availability of the structure of influenza neuraminidase .