Discussion: Notably, the presence of the A475V, L452R, V483A, and F490L mutations in the RBD domain of SARS-CoV-2 was shown to decrease the neutralizing activity of antibody and might impede the development of therapeutic antibodies (Li et al, 2020).
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: A348T, G476S, and V483A variants display reduced affinity to ACE2 in comparison to the Wuhan SARS-CoV2 spike protein.
Abstract: Evolutionary analysis reveals five RBD variants A348T, V367F, G476S, V483A, and S494P are under strong positive selection bias.
Method: Five RBD mutants were considered in the study (S494P, V483A, G476S, A348T, and V367F).
Result: Comparison of selection sites and alignment re
A therapeutic neutralizing antibody targeting receptor binding domain of SARS-CoV-2 spike protein.
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 of the S protein were mutated from histidine-to-tyrosine, valine-to-phenylalanine, glycine-to-serine, valine-to-alanine, aspartic-acid-to-glycine, or cysteine-to-alanine, respectively, were created by inserting overlapping PCR fragments into Acc65I/NotI-digested pCAGGS.
Method: The structural models of the
Genomic mutations and changes in protein secondary structure and solvent accessibility of SARS-CoV-2 (COVID-19 virus).
Conclusion: Alternatively, mutations H146Y (24 cases), V483A (11 cases), E554D (14 cases), P681L (16 cases) and S939F (11 cases) all occur only in USA or mutation L8V (4 cases) occurs only in Hong Kong (refer to the spreadsheet data, which can be found in the Data Availability section).
Conclusion: In the RBD region, S477G [CBCTT(S)CCCCC CBCTT(S)CCCEC], P479L [CTTSC(C)CCCCC CTTSC(C)CECCC], V483A [CCCCC(C)CTTTC CCCCC(C)CCTTC], and F486L [CCCCT(T)TCBCS CCCEC(T)TCBCS] are four mutations having protein structure change potential.
Conclusion: Notable mutation in this region is PMID: 33589648
2021
Communications biology
Result: Although mutatin A475V on the RBM has a negative binding free energy change with a relatively high frequency (5) on the RBM, the much higher frequencies of two mutations G476S (7) and V483A (31) with positive binding free energy change suggests that the mutations in Cluster C may strengthen the infectivity of SARS-CoV-2 in general.
Result: Mutation 23010T>C-(V483A) has the highest frequency (31) localized on the RBM has the positive binding free energy change, which indicates that V483A is prevalent in COVID-19 patients' in the United States has a potential capacity to enhance the infectivity of SARS-CoV-2.
Result: Notably, the V483A mutation is localized on the RBM with the highest frequ
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: A348T, G476S, and V483A variants display reduced affinity to ACE2 in comparison to the Wuhan SARS-CoV2 spike protein.
Abstract: Evolutionary analysis reveals five RBD variants A348T, V367F, G476S, V483A, and S494P are under strong positive selection bias.
Method: Five RBD mutants were considered in the study (S494P, V483A, G476S, A348T, and V367F).
Result: Comparison of selection sites and alignment re
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
Result: Eleven spike mutations were not found associated with ORF8 variants: L8V/W, N234Q, Q239K, L452R, A475V, G476S, V483A, F490L, V615I/F, A831V and D839Y/N/E.
SARS-CoV-2 genomic surveillance in Costa Rica: Evidence of a divergent population and an increased detection of a spike T1117I mutation.
PMID: 33905892
2021
Infection, genetics and evolution
Result: In addition, no structural variants in the receptor-binding domain (RBD) of the Spike protein (N439K, T481I, V483A, E484E, N501Y nor G476S) were identified.
Revealing the threat of emerging SARS-CoV-2 mutations to antibody therapies.
Abstract: We unveil, for the first time, that high-frequency mutations R346K/S, N439K, G446V, L455F, V483F/A, E484Q/V/A/G/D, F486L, F490L/V/S, Q493L, and S494P/L might compromise some of mAbs in clinical trials.
SARS_CoV_2 mutation literature information.
PMID: 
2021
EMBO molecular medicine
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