Endomannosidase structure revealed
21 Feb 2012 by Evoluted New Media
The structure of an enzyme that hijacks human enzymes to reproduce and cause disease has been determined by scientists in York.
A team from the University of York used state-of-the-art synchrotron technology to reveal the three-dimensional structure of bacterial endomannosidase, which they used as a model for the human enzyme. This structure revealed how viruses like HIV and Hepatitis C play biological piggy-back, using our cellular machinery to replicate and cause disease.
“If we understand how the viruses use our enzymes, we can develop inhibitors that block the pathway they require, opening the door to drug developments,” said Professor Gideon Davies from the Department of Chemistry.
This group of viruses – which includes Dengue Fever and West Nile virus – are able to bypass the main pathway if inhibited, and replicate via a second using endomannosidase, so for treatment to be effective, both pathways need to be blocked.
“It was already known how to block the main pathway for these viruses but until now, this endomannosidase pathway had proved a considerable challenge to study,” said Davies.
“Combining international resources and expertise, we were able to determine the endomannosidase structure and this has revealed how we can block the bypass route, stopping the viruses from hijacking human enzymes,” said Spencer Williams, an associate professor form the University of Melbourne.
Davies hopes the work – published in Proceedings of the National Academy of Sciences (PNAS) – will lead beyond viruses and point the way towards similar treatments for other diseases, including cancer.
