Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/81793
Title: The flavivirus NS2B–NS3 protease–helicase as a target for antiviral drug development
Authors: Luo, Dahai
Vasudevan, Subhash
Lescar, Julien
Keywords: Dengue virus NS2B–NS3 protease
Crystal structures
Issue Date: 2015
Source: Luo, D., Vasudevan, S., & Lescar, J. (2015). The flavivirus NS2B–NS3 protease–helicase as a target for antiviral drug development. Antiviral Research, 118, 148-158.
Series/Report no.: Antiviral Research
Abstract: The flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein. The multiple roles played by the NS2B–NS3 protein in the virus life cycle makes it an attractive target for antiviral drug discovery. The N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. In addition, NS2B–NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response. Here, we review biochemical and structural advances on the NS2B–NS3 protein, including the network of interactions it forms with NS5 and NS4B and highlight recent drug development efforts targeting this protein.
URI: https://hdl.handle.net/10356/81793
http://hdl.handle.net/10220/40998
ISSN: 0166-3542
DOI: 10.1016/j.antiviral.2015.03.014
Rights: © 2016 Elsevier. This is the author created version of a work that has been peer reviewed and accepted for publication by Antiviral Research, Elsevier. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1016/j.antiviral.2015.03.014].
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:LKCMedicine Journal Articles
SBS Journal Articles

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