A Study on Non-Synonymous Mutational Patterns in Structural Proteins of SARS-COV-2

Abstract

SARS-CoV-2 is mutating and creating divergent variants across the world. An in-depth investigation of the amino acid substitution in the genomic signature of SARS-CoV-2 proteins is highly essential for understanding its host adaptation and infection biology. A total of 9587 SARS-CoV-2 structural protein sequences collected from 49 different countries are used to characterize protein-wise variants, substitution pattern (type and location), and major substitution changes. The majority of the substitutions are distinct, occurred mostly in a particular location, and leads to a change in amino acid's biochemical properties. In terms of mutational changes, Envelope (E) and Membrane (M) proteins are relatively stable than Nucleocapsid (N) and Spike (S) proteins. Several co-occurrence substitutions are observed, particularly in S and N proteins. Substitution specific to active sub-domains reveals that Heptapeptide Repeat, Fusion peptides, Transmembrane in S protein, and N-terminal and C-terminal domains in N protein are remarkably mutated, and also found few deleterious mutations in these domains.

Structural and functional characterization of SARS-CoV-2 nucleocapsid protein mutations identified in Turkey by using in silico approaches

“…NTD and CTD regions of N protein are known to be involved in RNA binding (Zeng et al, 2020). In a recent study, by using the PROVEAN network server, 13 and 12 deleterious mutations are detected in the CTD and NTD domain of the N protein, respectively (Das and Roy, 2021). The deleterious D128y and P151S mutations in NTD and T334I and T271I mutations in CTD are consistent with our study.…”