Researchers from Durham University’s Centre for Bioactive Chemistry are developing methods that show how proteins interact with cell membranes when a virus strikes. Using their approach, the team hopes to find new ways to disrupt and disarm ‘enveloped viruses’ before they spread in our bodies.
Team members, Dr John Sanderson and Dr Paul Yeo from Durham University have helped produce the first ever, high-resolution, full-length structure of a protein from an enveloped virus called the ‘matrix protein’.
Viruses work in many different ways but in this case, respiratory syncytial virus (RSV) virions form by a ‘budding’ process at the plasma membrane of a cell. The matrix protein appears to drive the final assembly process and the formation of viral filaments. It is also clear that the matrix protein is an important determinant of where the virus buds.
Using x-ray crystallography, the team’s been able to see the intimate details of the matrix protein that controls how the RSV virus assembles inside a cell. The technique allows them to see how the virus protein functions and this could help the team to develop biochemical tools to treat respiratory ailments and the common cold.
Dr Yeo said: “We can now see what the protein virus structure looks like and we plan to pull the protein apart to see how and where it might be intercepted. These images provide amazing insights into the micro-chemical world of our cells. We have an opportunity to use bioactive chemistry to develop the medical tools of the future.”