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Biochem J. 2006 Jan 15;393(Pt 2):e1-3.

Unexpected similarity between the cytosolic West Nile virus NS3 and the secretory furin-like serine proteinases.

Author information

1
Laboratory of Biochemical Neuroendocrinology, Clinical Research Institute of Montreal, 110 Pine Ave West, Montreal, QC, H2W 1R7, Canada. seidahn@ircm.qc.ca

Abstract

Many viral proteins undergo proteolytic processing events that are required for virus infection and virion assembly. In this issue of Biochemical Journal, Strongin 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 led to the demonstration that furin/PC inhibitors containing poly(D-arginine) are also potent inhibitors of NS3, and that anthrax toxin protective antigen and myelin basic protein are potential NS3 substrates. Structural modelling based on Dengue virus NS3 provided a possible rationale for the observed cleavage specificity of West Nile virus NS3.

PMID:
16371006
PMCID:
PMC1360712
DOI:
10.1042/BJ20051787
[Indexed for MEDLINE]
Free PMC Article

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