Method: The SARS-CoV-2 S mutants (pC-SARS2-S-H49Y, pC-SARS2-S-V367F, pC-SARS2-S-G476S, pC-SARS2-S-V483A, pC-SARS2-S-D614G, or pC-SARS2-S-C1247A), in which positions 49, 367, 476, 483, 614, or 1247 o
Figure: V367F; the substitution from a valine to a phenylalanine at position 367 in the RBD introduces a larger side chain at a protomer-protomer interface, which might provide a more rigid RBD structure.
Genomic mutations and changes in protein secondary structure and solvent accessibility of SARS-CoV-2 (COVID-19 virus).
Introduction: Among them, there are three mutations occurring in the RBD region of the spike surface glycoprotein S, including N354D, D364Y and V367F, with the numbers showing amino acid (AA) positions in the protein.
Table: V367F
Analysis of SARS-CoV-2 mutations in the United States suggests presence of four substrains and novel variants.
Result: Although away from the RBM, the relatively high-frequency and positive binding free energy changes of V367F, R403K, and A411S indicate that more attention should be paid to them in the future.
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
Abstract: Evolutionary analysis reveals five RBD variants A348T, V367F, G476S, V483A, and S494P are under strong positive selection bias.
Abstract: 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.
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
SARS-CoV-2 variants combining spike mutations and the absence of ORF8 may be more transmissible and require close monitoring.
PMID: 33676232
2021
Biochemical and biophysical research communications
Table: V367F
IgV somatic mutation of human anti-SARS-CoV-2 monoclonal antibodies governs neutralization and breadth of reactivity.
Method: Alternatively, lentivirus Lenti-GF1-SARS-CoV-2Delta19AA truncated spike envelope displaying the H49Y, S247R, V367F, R408I, V483A, H519Q, A520S, and D614G mutations was produced using the same method.
Result: To determine if natural infection induced broadly neutralizing Abs, we tested neutralization of pseudotyped viruses with spike protein variants in the S1 N-terminal domain (H49Y, V247R, V367F, R408I), in the receptor-binding domain ( PMID: 33778182
2021
Gene reports
Discussion: Moreover, the D614G showed the highest host entry activity among mutations such as V367F, G476S, V483A, and H49Y that frequently occur in the S protein.
Unraveling the stability landscape of mutations in the SARS-CoV-2 receptor-binding domain.
Result: Mutation V367F was reported in 12 countries and appeared in 51 sequences.
Result: The 2-point mutation (V367F G413V) that was reported in Spain appears to have evolved from the widely spread mutated sequence (V367F) reported in 12 countries.
Table: V367F
The Impact on Infectivity and Neutralization Efficiency of SARS-CoV-2 Lineage B.1.351 Pseudovirus.
Method: Subsequently, SARS-CoV-2 Spike variants (D614G, V367F/D614G, P384L/D614G, R408I/D614G, N501Y/D614G, K417N/N501Y/D614G, E484K/N501Y/D614G) were generated using a Quikchange XL site-directed mutagenesis kit (Agilent, Santa Clara, CA, USA) according to manufacturer's instructions.
Method: The primers used to generate SARS-CoV-2 Spike variants are described as follow: PMID: 33976134
2021
Nature communications
Result: Another three are in moderately conserved contexts (V367F, D839Y/N/E, D936Y/H) less likely to be functional, and eight lie in repeatedly-altered amino acids in poorly conserved regions and are more likely to be neutral.
SARS_CoV_2 mutation literature information.
PMID: 
2021
Nature communications
Browser Board
Co-occurred Entities
Filtrator
ViMRT