Preprint Communication Version 1 Preserved in Portico This version is not peer-reviewed

Evolutionary Insights into the Envelope Protein of SARS-CoV-2

Version 1 : Received: 28 August 2020 / Approved: 30 August 2020 / Online: 30 August 2020 (11:50:59 CEST)

How to cite: Rahman, M.S.; Hoque, M.N.; Islam, M.R.; Islam, I.; Mishu, I.D.; Rahaman, M.M.; Sultana, M.; Hossain, M.A. Evolutionary Insights into the Envelope Protein of SARS-CoV-2. Preprints 2020, 2020080665 (doi: 10.20944/preprints202008.0665.v1). Rahman, M.S.; Hoque, M.N.; Islam, M.R.; Islam, I.; Mishu, I.D.; Rahaman, M.M.; Sultana, M.; Hossain, M.A. Evolutionary Insights into the Envelope Protein of SARS-CoV-2. Preprints 2020, 2020080665 (doi: 10.20944/preprints202008.0665.v1).

Abstract

The ongoing mutations in the structural proteins of SARS-CoV-2 is the major impediment for prevention and control of the COVID-19 disease. The envelope (E) protein of SARS-CoV-2 is a structural protein existing in both monomeric and homopentameric forms, associated with a multitude of functions including virus assembly, replication, dissemination, release of virions, infection, pathogenesis, and immune response stimulation. In the present study, 81,818 high quality E protein sequences retrieving from the GISAID were subjected to mutational analyses. Our analysis revealed that only 0.012 % (982/81818) stains possessed amino acid (aa) substitutions in 63 sites of the genome while 58.77% mutations in the primary structure of nucleotides in 134 sites. We found the V25A mutation in the transmembrane domain which is a key factor for the homopentameric conformation of E protein. We also observed a triple cysteine motif harboring mutations (L39M, A41S, A41V, C43F, C43R, C43S, C44Y, N45R) which may hinder the binding of E protein with spike glycoprotein. These results therefore suggest the continuous monitoring of each structural protein of SARS-CoV-2 since the number of genome sequences from across the world are continuously increasing.

Subject Areas

SARS-CoV-2; envelop protein; mutations; transmembrane domain; triple cysteine motif

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