A total of 22 N-glycosylation sites are present in S protein of SARS-CoV and SARS-CoV-2 at similar positions. The monomeric S protein consists of a large ectodomain, a single-pass transmembrane anchor, and a short intracellular tail at C-terminus. The S proteins (~ 1200 aa) are class-I viral fusion proteins and exist as trimers with two of the receptor binding sites (RBDs) facing “up” and the third RBD facing “down”.

An envelope-anchored SARS-CoV-2 spike (S) glycoprotein facilitates coronavirus entry into host cells. The virus has four structural proteins, known as S (spike), E (envelope), M (membrane), and N (nucleocapsid) proteins. The RNA genome of SARS-CoV-2 consists of 29,811 nucleotides, encodes 29 proteins and phylogenetic analysis suggests bat origin. The SARS-CoV-2 virions are 50−200 nm in diameter.

The disease caused by SARS-CoV-2 is called Corona Virus Disease 2019 (COVID-19). Both SARS-CoV and SARS-CoV-2 belong to the β-genus and lineage B ((β-B coronaviruses). β-coronaviruses are further divided into 4 lineages A, B, C, and D. Coronaviruses (CoVs) are largest RNA virus family divided into α, β, δ and γ genera. Specifically, the envelope and nucleocapsid proteins of SARS-CoV and SARS-CoV-2 share 96% and 89.6% sequence identities, respectively. Its genome is about 82% identical to the SARS coronavirus (SARS-CoV). In December 2019, a novel coronavirus SARS-CoV-2 (also known as 2019-nCoV) caused an outbreak of pulmonary disease in the city of Wuhan, China, and has since spread globally. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.Ĭompeting interests: The authors have declared that no competing interests exist. 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.ĭata Availability: All relevant data are within the manuscript and its Supporting Information files.įunding: We would like to acknowledge the Ramalingaswami Fellowship (BT/RLF/Reentry/ 64/2017), Department of Biotechnology, Govt of India (VK). Received: JAccepted: SeptemPublished: October 1, 2020Ĭopyright: © 2020 Jaiswal, Kumar. Abel, University of Tennessee, UNITED STATES Citation: Jaiswal G, Kumar V (2020) In-silico design of a potential inhibitor of SARS-CoV-2 S protein.

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