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A study on non-synonymous mutational patterns in structural proteins of SARS-CoV-2.
Genome. 2021 Jul; 64(7):665-678.G

Abstract

SARS-CoV-2 is mutating and creating divergent variants across the world. An in-depth investigation of the amino acid substitutions 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 patterns (type and location), and major substitution changes. The majority of the substitutions are distinct, mostly in a particular location, and lead to a change in an amino acid's biochemical properties. In terms of mutational changes, envelope (E) and membrane (M) proteins are relatively more 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 the N protein are remarkably mutated. We also observe a few deleterious mutations in the above domains. The overall study on non-synonymous mutation in structural proteins of SARS-CoV-2 at the start of the pandemic indicates a diversity amongst virus sequences.

Authors+Show Affiliations

Department of Pediatrics, Johns Hopkins University School of Medicine, Maryland, USA.Network Reconstruction & Analysis (NetRA) Lab, Department of Computer Applications, Sikkim University, Gangtok, India.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

33788636

Citation

Das, Jayanta Kumar, and Swarup Roy. "A Study On Non-synonymous Mutational Patterns in Structural Proteins of SARS-CoV-2." Genome, vol. 64, no. 7, 2021, pp. 665-678.
Das JK, Roy S. A study on non-synonymous mutational patterns in structural proteins of SARS-CoV-2. Genome. 2021;64(7):665-678.
Das, J. K., & Roy, S. (2021). A study on non-synonymous mutational patterns in structural proteins of SARS-CoV-2. Genome, 64(7), 665-678. https://doi.org/10.1139/gen-2020-0157
Das JK, Roy S. A Study On Non-synonymous Mutational Patterns in Structural Proteins of SARS-CoV-2. Genome. 2021;64(7):665-678. PubMed PMID: 33788636.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A study on non-synonymous mutational patterns in structural proteins of SARS-CoV-2. AU - Das,Jayanta Kumar, AU - Roy,Swarup, Y1 - 2021/03/31/ PY - 2021/4/1/pubmed PY - 2021/7/10/medline PY - 2021/3/31/entrez KW - acide aminé KW - amino acid KW - biochemical properties KW - caractéristiques des substitutions KW - functional sub-domains KW - mutation KW - propriétés biochimiques KW - protéines structurales KW - sous-domaines fonctionnels KW - structural proteins KW - substitution pattern SP - 665 EP - 678 JF - Genome JO - Genome VL - 64 IS - 7 N2 - SARS-CoV-2 is mutating and creating divergent variants across the world. An in-depth investigation of the amino acid substitutions 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 patterns (type and location), and major substitution changes. The majority of the substitutions are distinct, mostly in a particular location, and lead to a change in an amino acid's biochemical properties. In terms of mutational changes, envelope (E) and membrane (M) proteins are relatively more 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 the N protein are remarkably mutated. We also observe a few deleterious mutations in the above domains. The overall study on non-synonymous mutation in structural proteins of SARS-CoV-2 at the start of the pandemic indicates a diversity amongst virus sequences. SN - 1480-3321 UR - https://www.unboundmedicine.com/medline/citation/33788636/A_study_on_non_synonymous_mutational_patterns_in_structural_proteins_of_SARS_CoV_2_ L2 - https://cdnsciencepub.com/doi/abs/10.1139/gen-2020-0157?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -