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Insilico study on the effect of SARS-CoV-2 RBD hotspot mutants' interaction with ACE2 to understand the binding affinity and stability.
Virology. 2021 09; 561:107-116.V

Abstract

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 RBD-ACE2 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.

Authors+Show Affiliations

School of Computational and Integrative Sciences, Jawaharlal Nehru University, New Delhi, 110067, India. Electronic address: jyoti32_sit@jnu.ac.in.School of Computational and Integrative Sciences, Jawaharlal Nehru University, New Delhi, 110067, India. Electronic address: nsrao.jnu@gmail.com.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

34217923

Citation

Verma, Jyoti, and Naidu Subbarao. "Insilico Study On the Effect of SARS-CoV-2 RBD Hotspot Mutants' Interaction With ACE2 to Understand the Binding Affinity and Stability." Virology, vol. 561, 2021, pp. 107-116.
Verma J, Subbarao N. Insilico study on the effect of SARS-CoV-2 RBD hotspot mutants' interaction with ACE2 to understand the binding affinity and stability. Virology. 2021;561:107-116.
Verma, J., & Subbarao, N. (2021). Insilico study on the effect of SARS-CoV-2 RBD hotspot mutants' interaction with ACE2 to understand the binding affinity and stability. Virology, 561, 107-116. https://doi.org/10.1016/j.virol.2021.06.009
Verma J, Subbarao N. Insilico Study On the Effect of SARS-CoV-2 RBD Hotspot Mutants' Interaction With ACE2 to Understand the Binding Affinity and Stability. Virology. 2021;561:107-116. PubMed PMID: 34217923.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Insilico study on the effect of SARS-CoV-2 RBD hotspot mutants' interaction with ACE2 to understand the binding affinity and stability. AU - Verma,Jyoti, AU - Subbarao,Naidu, Y1 - 2021/06/28/ PY - 2021/03/26/received PY - 2021/06/16/revised PY - 2021/06/23/accepted PY - 2021/7/5/pubmed PY - 2021/7/27/medline PY - 2021/7/4/entrez KW - COVID-19 KW - Hotspot residues KW - Mutation KW - RBD-ACE2 interactions KW - Receptor binding domain KW - SARS-CoV-2 KW - SARS-CoV-2 variants KW - Spike protein SP - 107 EP - 116 JF - Virology JO - Virology VL - 561 N2 - 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 RBD-ACE2 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. SN - 1096-0341 UR - https://www.unboundmedicine.com/medline/citation/34217923/Insilico_study_on_the_effect_of_SARS_CoV_2_RBD_hotspot_mutants'_interaction_with_ACE2_to_understand_the_binding_affinity_and_stability_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0042-6822(21)00139-2 DB - PRIME DP - Unbound Medicine ER -