The flavivirus NS2B–NS3 protease–helicase as a target for antiviral drug development
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...
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sg-ntu-dr.10356-817932020-11-01T05:11:12Z The flavivirus NS2B–NS3 protease–helicase as a target for antiviral drug development Luo, Dahai Vasudevan, Subhash Lescar, Julien School of Biological Sciences Lee Kong Chian School of Medicine (LKCMedicine) Dengue virus NS2B–NS3 protease Crystal structures 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. MOE (Min. of Education, S’pore) NMRC (Natl Medical Research Council, S’pore) Accepted version 2016-07-27T02:40:08Z 2019-12-06T14:40:36Z 2016-07-27T02:40:08Z 2019-12-06T14:40:36Z 2015 Journal Article 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. 0166-3542 https://hdl.handle.net/10356/81793 http://hdl.handle.net/10220/40998 10.1016/j.antiviral.2015.03.014 en Antiviral Research © 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]. 29 p. application/pdf |
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Dengue virus NS2B–NS3 protease Crystal structures Luo, Dahai Vasudevan, Subhash Lescar, Julien The flavivirus NS2B–NS3 protease–helicase as a target for antiviral drug development |
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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. |
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School of Biological Sciences |
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School of Biological Sciences Luo, Dahai Vasudevan, Subhash Lescar, Julien |
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Article |
author |
Luo, Dahai Vasudevan, Subhash Lescar, Julien |
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Luo, Dahai |
title |
The flavivirus NS2B–NS3 protease–helicase as a target for antiviral drug development |
title_short |
The flavivirus NS2B–NS3 protease–helicase as a target for antiviral drug development |
title_full |
The flavivirus NS2B–NS3 protease–helicase as a target for antiviral drug development |
title_fullStr |
The flavivirus NS2B–NS3 protease–helicase as a target for antiviral drug development |
title_full_unstemmed |
The flavivirus NS2B–NS3 protease–helicase as a target for antiviral drug development |
title_sort |
flavivirus ns2b–ns3 protease–helicase as a target for antiviral drug development |
publishDate |
2016 |
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https://hdl.handle.net/10356/81793 http://hdl.handle.net/10220/40998 |
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