Journal of Virology & Antiviral ResearchISSN: 2324-8955

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Identification of Inhibitors Binding Site of Ebola L Polymerase Based on its Homology Model

This paper describes methods, results and conclusions about our study regarding the development and the optimization of a homology model of Ebola virus RNAdependent RNA polymerase, also called L polymerase, based on crystal structure of Vesicular stomatitis virus L polymerase. L polymerase is an essential protein for the outliving of virus; for this reason it is used as target for antiviral therapy. The aim of this work was to study the three-dimensional model of Ebola virus L polymerase and its inhibitors adopting a computational approach. We used docking simulation and multi-aligned L protein sequences in order to identify the potential binding pocket of inhibitors and their drug ability against Ebola virus L protein. Based on a dataset of ten validated molecules it was possible to understand the mechanism of action of potential inhibitors. The compounds analyzed were commercially purchasable, and experimentally tested, and the results obtained by our in silico analysis fit strongly with experimental data. This work summarizes the status quo of antiviral compounds currently used for Ebola virus disease

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