Analysis and comparison of physiochemical properties, mutations and glycosylation patterns between RNA polymerase and membrane protein of SARS-CoV and SARS-CoV-2.

Abstract

SARS-CoV-2 is a member of β-genus of the coronavirus subfamily, alongside the virus that causes SARS (Severe Acute Respiratory Syndrome). As implied by their names, SARS-CoV-2 and SARS-CoV genome sequences have close kinship (about 79% genomic sequence similarity). In the current research, sequence-based physiochemical properties of RNA polymerase and membrane glycoprotein of SARS-CoV-2 and SARS-CoV were compared. In addition, impacts of substitution mutations on stability and glycosylation patterns of these proteins were studied. In comparison of physiochemical features of membrane and RNA polymerase proteins, only instability index of membrane protein was difference between SARS-CoV and SARS-CoV-2. Mutation analysis showed increase in stability of RNA polymerase and decrease in stability of membrane protein in SARS-CoV-2. Glycosylation pattern analysis showed glycosylation enhancement in both membrane and RNA polymerase proteins of SARS-CoV-2 in comparison to SARS-CoV. In conclusion, more glycosylation and stability of SARS-CoV-2 RNA polymerase could be one of the reasons of high pathogenicity property and host immune system evasion of SARS-CoV-2.