West Nile Disease Breakthrough
Now, there is a chance that a team of researchers have identified a promising drug target.
In the latest issue of the Biochemical Journal, Alex Strongin of The Burnam Institute, La Jolla, and co-workers report that the NS3 protease from West Nile virus unexpectedly cleaves certain substrates at pairs of basic residues, a specificity that resembles that of the furin-like PCs (proprotein convertases).
This suggests that furin/PC inhibitors containing poly(D-arginine) could be used as inhibitors of NS3, and that anthrax toxin protective antigen and myelin basic protein are potential NS3 substrates.
The hope is that the isolation of small-molecule inhibitors to WNV NS3 could at least lower the viral burden, and could lead to a clinically-effective drug.
An associated commentary is at:
biochemj.org/bj/393/e001/393e001.pdf
The Biochemical Journal is the flagship journal for the molecular life-science community in the UK and worldwide. The Biochemist is celebrating 100 years of scientific excellence in 2006.
The full paper is available at:
biochemj.org/bj/393/0503/3930503.pdf
Peer reviewed publication and references
Biochem. J. (2006) 393, 503-511 doi:10.1042/BJ20051374
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