LAUSR

Abstract Ebola is one of the most dangerous pathogenic RNA virus that causes severe hemorrhagic fever in humans and is considered to be a threat to humanity. The RNA genome of EBOV encodes seven proteins viz., glycoprotein (GP), nucleoprotein (NP), RNA-dependent RNA polymerase (protein ‘L’), VP35, VP30, VP40 andVP24. The objective of the present study is to find a suitable inhibitor for protein ‘L’. The large structural protein ‘L’, is made up of 2212 amino acid residues. This protein works as an RNA-dependent RNA polymerase (RdRp) and a methyl transferase. It is carried by the virus during the infection as the host mechanisms cannot be used to transcribe the –ss RNA genome of the virus. As the protein is crucial for the replication of the viral genome and no other host enzyme can perform the same function, this viral protein ‘L’ was considered as a potential drug target to design inhibitors. The 3D structure of protein ‘L’ is not available to date. This is a limitation in understanding the protein's function. Hence, the present work is aimed at predicting the first homology-based model of protein ‘L’ and elucidating the function by providing insight into the molecular details of the protein. As there is no drug available for the treatment of EBOV infection our findings play a crucial a role to identify an inhibitor of the protein ‘L’ of EBOV. HTS against ZINC database resulted in identification of few possible inhibitors. Molecular docking studies resulted in finding a suitable inhibitor for protein ‘L’.