Abstract: High-affinity RBD-specific antibodies exhibited high potency in neutralizing both live and pseudotype SARS-CoV-2 viruses and the SARS-CoV-2 pseudovirus particle containing the spike protein S-RBDV367F mutant (SARS-CoV-2(V367F)).
Introduction: Overall, these antibodies recognize four distinct epitopes on the RBD, and cocktails containing mAbs targeting different antigenic sites showed higher potency to neutralize the SARS-CoV-2 virus and SARS-CoV-2(V367F) pseudovirus particle.
Introduction: These antibodies exhibited a higher binding affinity to the RBD and high potency to neutralize both live and pseudotype SARS-CoV-2 viruses and SARS-CoV-2(V367F) pseudovir
Serum Neutralizing Activity of mRNA-1273 against SARS-CoV-2 Variants.
Discussion: Global data analysis shows that infectivity strengthening and virion stable mutations are on the rise (especially the frequency of S477N, N439K, V483A, and V367F), clearly indicating the natural selection of mutations with stronger transmissibility.
Organ-specific genome diversity of replication-competent SARS-CoV-2.
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: It is noteworthy that single amino acid changes such as Y145del, F490S, A831S and double amino acid changes including D614G+A879S, D614G+A879T, and D614G+M1237I were reported to be resistant to convalescent sera or these mutations could confer the S protein monoclonal antibody resistance, whereas V367F of the RBD was reported to have increased sensitivity to neutralizing antibodies.
Characterization of SARS-CoV-2 different variants and related morbidity and mortality: a systematic review.
PMID: 34103090
2021
European journal of medical research
Table: V367F
Systemic effects of missense mutations on SARS-CoV-2 spike glycoprotein stability and receptor-binding affinity.
Result: V483A in 24 strains have small effects (DeltaDeltaG = -0.196 kcal/mol) and V367F in 13 strains has moderate stabilizing effects (DeltaDeltaG = -0.597 kcal/mol) on RBD.
Result: The DeltaDeltaDeltaG of common variants V483A and V367F are close to 0, meaning that these mutations have no effects on binding affinity.
Table: V367F
Discussion: In addition, common viral mutations D936Y in 37 strains, V483A in 24 strains and V367F in 14 strains can also induce the stabilizing effects on SARS-Cov-2 full-length S or RBD (Table 3).
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
Conclusi
Conclusion: In V367F, the reorientation of Lys31 facilitates two additional hydrogen bonds formation which enhances its binding free energy contribution.
Conclusion: Interestingly, the V367F and S494P population variants display a higher binding affinity towards human ACE2.
Figure: Variations of root mean square deviation (RMSD) (A), Distribution of RBD-ACE2 distances (B), Distribution of RBD-ACE2 interfacial area (C), number of hydrogen bonds (D), van der Waals interaction energy (E), and electrostatic interactions energy (F) between RBD and ACE2 obtained from the molecular dynamics simulations for wild-type, V367F and S494P variant of RBD are shown.
A therapeutic neutralizing antibody targeting receptor binding domain of SARS-CoV-2 spike protein.
Method: Recombinant proteins for RBD and its mutants (A435S, F342L, G476S, K458R, N354D, V367F, V483A, W436R), SARS-CoV S1, HCoV-HKU1 S1, and MERS-CoV RBD were commercial products (Sino Biological).
Discussion: For instance, V367F, W436R, and D364Y were reported to increase the binding affinity for ACE2, which might accelerate viral spread further perpetuating the pandemic.
SARS_CoV_2 mutation literature information.
PMID: 
2021
MedComm
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