Homology modeling and molecular dynamics study of West Nile virus NS3 protease: A molecular basis for the catalytic activity increased by the NS2B cofactor

2006 ◽  
Vol 65 (3) ◽  
pp. 692-701 ◽  
Author(s):  
Hong Zhou ◽  
N. Jiten Singh ◽  
Kwang S. Kim
Keyword(s):  
Molecular Dynamics ◽  
Catalytic Activity ◽  
West Nile Virus ◽  
Homology Modeling ◽  
Molecular Basis ◽  
West Nile ◽  
Ns3 Protease

scholarly journals Potential Dual Role of West Nile Virus NS2B in Orchestrating NS3 Enzymatic Activity in Viral Replication

Viruses ◽  
2021 ◽  
Vol 13 (2) ◽  
pp. 216
Author(s):  
Alanna C. Tseng ◽  
Vivek R. Nerurkar ◽  
Kabi R. Neupane ◽  
Helmut Kae ◽  
Pakieli H. Kaufusi
Keyword(s):  
West Nile Virus ◽  
Enzymatic Activity ◽  
Nonstructural Protein ◽  
Antiviral Drug ◽  
West Nile ◽  
Biochemical Assays ◽  
In Trans ◽  
Viral Polyprotein ◽  
Ns3 Protease

West Nile virus (WNV) nonstructural protein 3 (NS3) harbors the viral triphosphatase and helicase for viral RNA synthesis and, together with NS2B, constitutes the protease responsible for polyprotein processing. NS3 is a soluble protein, but it is localized to specialized compartments at the rough endoplasmic reticulum (RER), where its enzymatic functions are essential for virus replication. However, the mechanistic details behind the recruitment of NS3 from the cytoplasm to the RER have not yet been fully elucidated. In this study, we employed immunofluorescence and biochemical assays to demonstrate that NS3, when expressed individually and when cleaved from the viral polyprotein, is localized exclusively to the cytoplasm. Furthermore, NS3 appeared to be peripherally recruited to the RER and proteolytically active when NS2B was provided in trans. Thus, we provide evidence for a potential additional role for NS2B in not only serving as the cofactor for the NS3 protease, but also in recruiting NS3 from the cytoplasm to the RER for proper enzymatic activity. Results from our study suggest that targeting the interaction between NS2B and NS3 in disrupting the NS3 ER localization may be an attractive avenue for antiviral drug discovery.

scholarly journals Phosphonate inhibitors of West Nile virus NS2B/NS3 protease

2018 ◽  
Vol 34 (1) ◽  
pp. 8-14 ◽  
Author(s):  
Marcin Skoreński ◽  
Aleksandra Milewska ◽  
Krzysztof Pyrć ◽  
Marcin Sieńczyk ◽  
Józef Oleksyszyn
Keyword(s):  
West Nile Virus ◽  
West Nile ◽  
Ns3 Protease

STD-NMR experiments identify a structural motif with novel second-site activity against West Nile virus NS2B-NS3 protease

2017 ◽  
Vol 146 ◽  
pp. 174-183 ◽  
Author(s):  
Tobias Schöne ◽  
Lena Lisbeth Grimm ◽  
Naoki Sakai ◽  
Linlin Zhang ◽  
Rolf Hilgenfeld ◽  
...  
Keyword(s):  
West Nile Virus ◽  
Structural Motif ◽  
West Nile ◽  
Std Nmr ◽  
Ns3 Protease

scholarly journals Peptide-β-lactam Inhibitors of Dengue and West Nile Virus NS2B-NS3 Protease Display Two Distinct Binding Modes

2019 ◽  
Vol 63 (1) ◽  
pp. 140-156 ◽  
Author(s):  
Tonko Dražić ◽  
Sara Kopf ◽  
James Corridan ◽  
Mila M. Leuthold ◽  
Branimir Bertoša ◽  
...  
Keyword(s):  
West Nile Virus ◽  
Binding Modes ◽  
West Nile ◽  
Ns3 Protease

Exploring the binding of peptidic West Nile virus NS2B–NS3 protease inhibitors by NMR

2013 ◽  
Vol 97 (2) ◽  
pp. 137-144 ◽  
Author(s):  
CongBao Kang ◽  
Shovanlal Gayen ◽  
Weiling Wang ◽  
Rene Severin ◽  
Angela Shuyi Chen ◽  
...  
Keyword(s):  
West Nile Virus ◽  
Protease Inhibitors ◽  
West Nile ◽  
Ns3 Protease Inhibitors ◽  
Ns3 Protease

Structure of West Nile Virus NS3 Protease: Ligand Stabilization of the Catalytic Conformation

2009 ◽  
Vol 385 (5) ◽  
pp. 1568-1577 ◽  
Author(s):  
Gautier Robin ◽  
Keith Chappell ◽  
Martin J. Stoermer ◽  
Shu-Hong Hu ◽  
Paul R. Young ◽  
...  
Keyword(s):  
West Nile Virus ◽  
West Nile ◽  
Ligand Stabilization ◽  
Ns3 Protease
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