scholarly journals Cover Picture: Development and Characterization of New Peptidomimetic Inhibitors of the West Nile Virus NS2B-NS3 Protease (ChemMedChem 2/2013)

ChemMedChem ◽  
2013 ◽  
Vol 8 (2) ◽  
pp. 173-173
Author(s):  
M. Zouhir Hammamy ◽  
Caroline Haase ◽  
Maya Hammami ◽  
Rolf Hilgenfeld ◽  
Torsten Steinmetzer
Keyword(s):  
West Nile Virus ◽  
The West ◽  
West Nile ◽  
Peptidomimetic Inhibitors ◽  
Ns3 Protease

scholarly journals Development and Characterization of New Peptidomimetic Inhibitors of the West Nile Virus NS2B-NS3 Protease

ChemMedChem ◽  
2013 ◽  
Vol 8 (2) ◽  
pp. 231-241 ◽  
Author(s):  
M. Zouhir Hammamy ◽  
Caroline Haase ◽  
Maya Hammami ◽  
Rolf Hilgenfeld ◽  
Torsten Steinmetzer
Keyword(s):  
West Nile Virus ◽  
The West ◽  
West Nile ◽  
Peptidomimetic Inhibitors ◽  
Ns3 Protease

Novel agmatine and agmatine-like peptidomimetic inhibitors of the West Nile virus NS2B/NS3 serine protease

2011 ◽  
Vol 46 (7) ◽  
pp. 3130-3134 ◽  
Author(s):  
Huichang Annie Lim ◽  
Joma Joy ◽  
Jeffrey Hill ◽  
Cheng San Brian Chia
Keyword(s):  
West Nile Virus ◽  
Serine Protease ◽  
The West ◽  
West Nile ◽  
Peptidomimetic Inhibitors

scholarly journals Mutagenesis of the West Nile virus NS2B cofactor domain reveals two regions essential for protease activity

2008 ◽  
Vol 89 (4) ◽  
pp. 1010-1014 ◽  
Author(s):  
Keith J. Chappell ◽  
Martin J. Stoermer ◽  
David P. Fairlie ◽  
Paul R. Young
Keyword(s):  
West Nile Virus ◽  
Proteolytic Activity ◽  
The West ◽  
West Nile ◽  
Mutagenesis Screen ◽  
Antiviral Compounds ◽  
Protease Activation ◽  
Primary Focus ◽  
Ns3 Protease

The flavivirus NS2B/NS3 protease has received considerable attention as a target for the development of antiviral compounds. While substrate based inhibitors have been the primary focus to date, an approach focussing on NS2B cofactor displacement could prove to be an effective alternative. To understand better the role of the NS2B cofactor in protease activation, we conducted an alanine mutagenesis screen throughout the 42-residue central cofactor domain (NS2B51–92) of West Nile virus (WNV). Two sites critical for proteolytic activity were identified (NS2B59–62 and NS2B75–87), where the majority of substitutions were found to significantly decrease proteolytic activity of a recombinant WNV NS2B/NS3 protease. These findings provide mechanistic insights into the structural and functional role that the cofactor may play in the substrate-bound and free protease complexes as well as providing novel sites for targeting new antiviral inhibitors.

Evolutionary characterization of the West Nile Virus complete genome

2010 ◽  
Vol 56 (1) ◽  
pp. 195-200 ◽  
Author(s):  
R.R. Gray ◽  
N.M.C. Veras ◽  
L.A. Santos ◽  
M. Salemi
Keyword(s):  
West Nile Virus ◽  
Complete Genome ◽  
The West ◽  
West Nile

Novel agmatine dipeptide inhibitors against the West Nile virus NS2B/NS3 protease: A P3 and N-cap optimization study

2013 ◽  
Vol 62 ◽  
pp. 199-205 ◽  
Author(s):  
Huichang Annie Lim ◽  
Melgious Jin Yan Ang ◽  
Joma Joy ◽  
Anders Poulsen ◽  
Wenshi Wu ◽  
...  
Keyword(s):  
West Nile Virus ◽  
The West ◽  
West Nile ◽  
Optimization Study ◽  
Ns3 Protease

Characterization of the West Nile virus protease substrate specificity and inhibitors

2007 ◽  
Vol 39 (3) ◽  
pp. 606-614 ◽  
Author(s):  
Niklaus H. Mueller ◽  
Changsuek Yon ◽  
Vannakambadi K. Ganesh ◽  
R. Padmanabhan
Keyword(s):  
West Nile Virus ◽  
Substrate Specificity ◽  
The West ◽  
West Nile ◽  
Protease Substrate
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