期刊
VIROLOGY
卷 561, 期 -, 页码 107-116出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2021.06.009
关键词
SARS-CoV-2; Mutation; Spike protein; Receptor binding domain; RBD-ACE2 interactions; COVID-19; Hotspot residues; SARS-CoV-2 variants
类别
资金
- University Grant Commission in the form of Junior Research Fellowship
Research shows that the variants of the novel coronavirus increase its binding affinity with human cells, thereby enhancing the virus's infectivity and pathogenicity. Understanding the impact of these mutations can help in the development of vaccines and treatments.
The fall of 2020 brought several new variants of SARS-CoV-2 circulating across the globe, and the steadily increasing COVID-19 cases are responsible for the emergence of these variants. All the SARS-CoV-2 variants reported to date have multiple mutations in the spike (S) protein, specifically in the receptor-binding domain (RBD). Here, we employed an integrated computational approach involving structure and sequence based predictions to study the effect of naturally occurring variations in the S-RBD on its stability and ACE2 binding affinity. The hotspot stabilizing residue mutations N501I, N501Y, Q493L, Q493H and K417R, strengthen the RBDACE2 complex by modulating the interaction statistics at the interface. Thus, we report here some critical mutations that could increase the binding affinity of the SARS-CoV-2 RBD with ACE2, increasing the viral infectivity and pathogenicity. Understanding the effect of these mutations will help in developing potential vaccines and therapeutics.
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