alexa The Vesicular Stomatitis Virus Glycoprotein as a Target for Antivirals and Docking of Dansylcadaverine | OMICS International | Abstract
ISSN: 1948-5964

Journal of Antivirals & Antiretrovirals
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Research Article

The Vesicular Stomatitis Virus Glycoprotein as a Target for Antivirals and Docking of Dansylcadaverine

Arpita Banerjee and Sarah S. Cherian*

National Institute of Virology, 20/A Dr. Ambedkar Road, Pune - 411001, Maharashtra, India

*Corresponding Author:
Dr. Sarah S. Cherian
National Institute of Virology
20/A Dr. Ambedkar Road
Pune, India-411001
Tel: 91-020-26006218
Fax: 91-020-26122669
E-mail: [email protected], [email protected]

Received Date: October 10, 2010; Accepted Date: October 16, 2010; Published Date: October 18, 2010

Citation: Banerjee A, Cherian SS (2010) The Vesicular Stomatitis Virus Glycoprotein as a Target for Antivirals and Docking of Dansylcadaverine. J Antivir Antiretrovir 2: 046-050. doi: 10.4172/jaa.1000022

Copyright: © 2010 Banerjee A, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

Rhabdoviruses include Vesicular stomatitis virus (VSV) and notable human pathogens such as the Rabies virus and the Chandipura virus. Modeling of target receptors and binding site identification is an important step in developing new therapeutic agents. Ligands that bind selectively to proteins of the membrane fusion pathway can retard or block viral entry. In this study, the surface glycoprotein G of the VSV was selected as a potential antiviral target. Dansylcadaverine, Rimantadine and Amantadine are known inhibitors which have been shown to prevent VSV internalization, though the molecular mechanism of their inhibition is not well understood. The potential of these ligands as fusion inhibitors was explored by undertaking in-silico binding site identification and docking studies. A ligand binding pocket was predicted in the G trimer interface. On docking, Dansylcadaverine made energetically favourable contacts with residue stretches required for the structural transition of the protein to the fusion active form while Rimantadine and Amantadine failed to dock into the binding pocket. Our results suggest that Dansylcadaverine could prevent viral entry by stabilizing the G protein in the prefusion conformation. The findings of this study can be extended to design antivirals against other viruses of the same family.

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