Biochem. J. (2006) 393
(e1–e3) (Printed in Great Britain)
Commentary
Unexpected similarity between the cytosolic West Nile virus NS3 and the secretory furin-like serine proteinases
Nabil G. SEIDAH1
Laboratory of Biochemical Neuroendocrinology, Clinical Research Institute of Montreal, 110 Pine Ave West, Montreal, QC, H2W 1R7, Canada
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.
Key words: cleavage specificity, furin, inhibitor, modelling, NS3 protease, West Nile virus.
1email seidahn@ircm.qc.ca
Received 7 November 2005; accepted 9 November 2005
Published on the Internet 23 December 2005, doi:10.1042/BJ20051787
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