Result: Of these, five (S477N, E484K, E484Q, S494L, S494P) were found in viruses circulating in Bengaluru, and the amino acid replacement V483A was from an imported case.
Discussion: All nine amino acid changes, namely N440K, S477N, V483A, E484K/Q, F490S, S494L/P, N501Y are associated with immune escape.
Phylodynamic Pattern of Genetic Clusters, Paradigm Shift on Spatio-Temporal Distribution of Clades, and Impact of Spike Glycoprotein Mutations of SARS-CoV-2 Isolates from India.
PMID: 35017872
2021
Journal of global infectious diseases
Result: Among the mutations in RBD, R346K, N440K, G446V, N450K, V483F, E484K, E484Q, F490S and S494P also showed change in ACE2 binding to the extent of 75% to 90%.
Result: Variants identified with mutations at sites such as E484 (E484Q), F490 (F490S), Q493 (Q493STOP), and S494 (S494P) in the RBD are presumed to have immune escape features.
Unraveling the stability landscape of mutations in the SARS-CoV-2 receptor-binding domain.
Evolutionary and structural analysis elucidates mutations on SARS-CoV2 spike protein with altered human ACE2 binding affinity.
PMID: 33272568
2021
Biochemical and biophysical research communications
Abstract: Evolutionary analysis reveals five RBD variants A348T, V367F, G476S, V483A, and S494P are under strong positive selection bias.
Abstract: On the other hand, the enhanced binding affinity of S494P is attributed to strong interfacial complementarity between the RBD and ACE2.
Abstract: While the V367F and S494P population variants display a higher binding affinity towards human ACE2.
Method: Five RBD mutants were considered in the study (S494P, V483A, G476S, PMID: 33535027
2021
Cell host & microbe
Result: The penetrance of the remaining substitutions among clinical isolates is relatively low, with G446V, T478I, E484K, S477I, and S494P ranking 79, 102, 123, 135, and 146 of the top 150 variants in S or roughly 0.05% of sequenced variants.
Genomic mutations and changes in protein secondary structure and solvent accessibility of SARS-CoV-2 (COVID-19 virus).
Evolutionary and structural analysis elucidates mutations on SARS-CoV2 spike protein with altered human ACE2 binding affinity.
PMID: 33602511
2021
Biochemical and biophysical research communications
Conclusion: Comparisons of selection sites reveal three RBM population variants G476S, V483A, and S494P that are in close contact with the ACE2 binding region.
Conclusion: Interestingly, the V367F and S494P population variants display a higher binding affinity towards human ACE2.
Conclusion: The enhanced binding affinity of S494P is attributed to strong interfacial complementarity during ACE2 recognition, while the V367F variant interacts with the ACE2 mediated by a higher number of hydrogen bonds.
Figure: Variations of root mean square deviation (RMSD) (A), Distribution of RBD-ACE2 distances (B), Distribution of RBD-ACE2 interfacial area (C), number of hydr
SARS-CoV-2 B.1.1.7 sensitivity to mRNA vaccine-elicited, convalescent and monoclonal antibodies.
Result: The escape mutations present at the highest frequency among sequenced isolates are E484K, L452R, and S494P for LY-CoV555, and K417N/T for LY-CoV016.
Neutralising antibody escape of SARS-CoV-2 spike protein: Risk assessment for antibody-based Covid-19 therapeutics and vaccines.
SARS_CoV_2 mutation literature information.
PMID: 
2021
Wellcome open research
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