By solving the structure of the Foot-and-Mouth Disease Virus (FMDV) enzyme named '3C protease' scientists have taken an essential step towards developing protease inhibitors, a class of anti-viral drug that has proved hugely successful in controlling HIV.

The structure paves the way for their development by revealing the atomic details of the key viral enzyme that would serve as a target for drugs.

3C protease's function is to help the virus replicate itself. A drug that binds and inhibits FMDV 3C protease would stop its spread by blocking its replication and thus its ability to infect a herd.

"In an outbreak we would 'dose up' the animals and in theory they would be protected immediately," said Dr Stephen Curry of Imperial College London and senior author of the research paper, published in Journal of Biological Chemistry this week. "In contrast, vaccines take several days to have effect and that allows further spread of the disease."

"Our work is a very first step in developing an effective drug to do this. We can see what the enzyme looks like and it gives us an idea of what sort of shapes and types of molecule could bind specifically to the enzyme and block it."

The Imperial researchers are now designing a molecule to act as an inhibitor.

Together with Professor Robin Leatherbarrow of the Department of Chemistry, Dr Curry's team from the Division of Cell and Molecular Biology has probed the specificity of the 3C enzyme in the hope of developing peptide-like inhibitors, similar to those successful in tackling HIV. Professor Leatherbarrow is mapping out the key amino acid sequences that the protease snips in-between, a process called 'peptide cleavage analysis'.

"We've determined the key features
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Contact: Tom Miller
t.miller@imperial.ac.uk
44-207-594-6704
Imperial College London
21-Mar-2005