ArticleBiochemical and biophysical research communications2021
Evolutionary and structural analysis elucidates mutations on SARS-CoV2 spike protein with altered human ACE2 binding affinity.
Article in Biochemical and biophysical research communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Article
- Review
- Current Updates on Variants of SARS-CoV- 2: Systematic Review.Health science reports · 2024Review
- The Malaria Box molecules: a source for targeting the RBD and NTD cryptic pocket of the spike glycoprotein in SARS-CoV-2.Journal of molecular modeling · 2024Article
- Predicting Natural Evolution in the RBD Region of the Spike Glycoprotein of SARS-CoV-2 by Machine Learning.Viruses · 2024Article
- Alterations of SARS-CoV-2 Evolutionary Dynamics by Pharmaceutical Factors.Infectious diseases & immunity · 2024Review
- Early Emerging SARS-CoV-2 Spike Mutants Are Diversified in Virologic Properties but Elicit Compromised Antibody Responses.Viruses · 2023Article
- Article
- An integrated understanding of the evolutionary and structural features of the SARS-CoV-2 spike receptor binding domain (RBD).International journal of biological macromolecules · 2022Article
- Healthy humans can be a source of antibodies countering COVID-19.Bioengineered · 2022Article
- Structure/Function Analysis of Truncated Amino-Terminal ACE2 Peptide Analogs That Bind to SARS-CoV-2 Spike Glycoprotein.Molecules (Basel, Switzerland) · 2022Article
- Screening of potential spike glycoprotein / ACE2 dual antagonists against COVID-19 in silico molecular docking.Journal of virological methods · 2022Article
- An engineered bispecific human monoclonal antibody against SARS-CoV-2.Nature immunology · 2022Article
- COVID-19 in an immunocompromised host: persistent shedding of viable SARS-CoV-2 and emergence of multiple mutations: a case report.International journal of infectious diseases : IJID : official publication of the International Society for Infectious Diseases · 2022Article
- Mutation-induced changes in the receptor-binding interface of the SARS-CoV-2 Delta variant B.1.617.2 and implications for immune evasion.Biochemical and biophysical research communications · 2021Article
- Natto extract, a Japanese fermented soybean food, directly inhibits viral infections including SARS-CoV-2 in vitro.Biochemical and biophysical research communications · 2021Article
- Article
- Preliminary report on severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Spike mutation T478K.Journal of medical virology · 2021Article
- Lower Gene Expression of Angiotensin Converting Enzyme 2 Receptor in Lung Tissues of Smokers with COVID-19 Pneumonia.Biomolecules · 2021Article
- Host variations in SARS-CoV-2 infection.Turkish journal of biology = Turk biyoloji dergisi · 2021Review
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Abstract
The recognition of ACE2 by the receptor-binding domain (RBD) of spike protein mediates host cell entry. The objective of the work is to identify SARS-CoV2 spike variants that emerged during the pandemic and evaluate their binding affinity with ACE2. Evolutionary analysis of 2178 SARS-CoV2 genomes identifies RBD variants that are under selection bias. The binding efficacy of these RBD variants to the ACE2 has been analyzed by using protein-protein docking and binding free energy calculations. Pan-proteomic analysis reveals 113 mutations among them 33 are parsimonious. Evolutionary analysis reveals five RBD variants A348T, V367F, G476S, V483A, and S494P are under strong positive selection bias. Variations at these sites alter the ACE2 binding affinity. A348T, G476S, and V483A variants display reduced affinity to ACE2 in comparison to the Wuhan SARS-CoV2 spike protein. While the V367F and S494P population variants display a higher binding affinity towards human ACE2. Reorientation of several crucial residues at the RBD-ACE2 interface facilitates additional hydrogen bond formation for the V367F variant which enhances the binding energy during ACE2 recognition. On the other hand, the enhanced binding affinity of S494P is attributed to strong interfacial complementarity between the RBD and ACE2.
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