April 1 2020

A team of researchers from the ARC Centre of Excellence in Advanced Molecular Imaging (Imaging CoE) and the Monash Biomedicine Discovery Institute (BDI) have determined the 3-D structure of one of the proteins produced by the novel coronavirus COVID-19. In order to make the structure available to the worldwide community, the data has been released on the pre-print journal, bioRxiv, and is currently undergoing peer review.

In order to design drugs against the coronavirus, scientists need to know what the protein components of the virus look like. There is a global effort underway to determine the structure of the 27 proteins produced by COVID-19. This information will underpin the development of future therapies to block any of these proteins, killing the virus or slowing its spread.

Now a team of Imaging CoE researchers from the Monash University Node, using the Australian Synchrotron, have determined the 3D-structure of the COVID-19 non-structural protein 9 (Nsp9) protein at atomic resolution. The function of Nsp9 is still not fully understood, however, studies on the related SARS virus suggests that it may function in viral replication.

Dr Dene Littler, within the laboratory of Prof. Jamie Rossjohn from the Imaging CoE, have been examining some of the lesser-understood proteins produced by SARS-CoV-2.

According to Prof. Rossjohn: “scientists will now study the structure and function of all of the proteins produced by the COVID-19 virus in order to work out the best strategy for developing new drugs to prevent the virus from replicating.”

Prof. Rossjohn added: “this represents the start of an accelerated program of research within Monash that is aimed at developing new anti-viral treatments as well as understanding how the immune system combats this virus.

“When you are battling a dangerous virus like coronavirus, you need as many weapons in your armoury as possible.”