West Nile Virus NS2B/NS3 protease as an antiviral target

Chappell, K. J., Stoermer, M. J., Fairlie, D. P. and Young, P. R. (2008) West Nile Virus NS2B/NS3 protease as an antiviral target. Current Medicinal Chemistry, 15 27: 2771-2784. doi:10.2174/092986708786242804

Author Chappell, K. J.
Stoermer, M. J.
Fairlie, D. P.
Young, P. R.
Title West Nile Virus NS2B/NS3 protease as an antiviral target
Journal name Current Medicinal Chemistry   Check publisher's open access policy
ISSN 0929-8673
Publication date 2008-11-01
Year available 2008
Sub-type Article (original research)
DOI 10.2174/092986708786242804
Open Access Status Not yet assessed
Volume 15
Issue 27
Start page 2771
End page 2784
Total pages 14
Editor Atta-ur Rahman
Place of publication Oak Park, IL., U.S.A.
Publisher Bentham Science Publishers
Language eng
Subject C1
060506 Virology
110309 Infectious Diseases
970106 Expanding Knowledge in the Biological Sciences
920412 Preventive Medicine
030403 Characterisation of Biological Macromolecules
030499 Medicinal and Biomolecular Chemistry not elsewhere classified
Abstract West Nile Virus (WNV) has spread rapidly during the last decade across five continents causing disease and fatalities in humans and mammals. It highlights the serious threat to both our health and the economy posed by viruses crossing species, in this case from migratory birds via mosquitoes to mammals. There is no vaccine or antiviral drug for treating WNV infection. One attractive target for antiviral development is a viral trypsin-like serine protease, encoded by the N-terminal 184 amino acids of NS3, which is only active when tethered to its cofactor, NS2B. This protease, NS2B/NS3pro, cleaves the viral polyprotein to release structural and non-structural viral proteins that are essential in viral replication and assembly of new virus particles. Disruption of this protease activity is lethal for virus replication. The NS3 protein also has other enzymes within its sequence (helicase, nucleoside triphosphatase, RNA triphosphatase), all of which are tightly regulated through localisation within membranous compartments in the infected cell. This review describes the various roles of NS3, focussing on NS2B-NS3 protease and its function and regulation in WNV replication and infection. Current advances towards development of antiviral inhibitors of NS2B/NS3pro are examined along with obstacles to their development as an antiviral therapy. © 2008 Bentham Science Publishers Ltd
Keyword West Nile Virus
Serine protease
Hepatitis C virus
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

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Created: Fri, 20 Mar 2009, 23:21:17 EST by Jennifer Falknau on behalf of Institute for Molecular Bioscience