Comprehensive annotations of the mutational spectra of SARS-CoV-2 spike protein: a fast and accurate pipeline.
PMID: 32954666
2021
Transboundary and emerging diseases
Result: We also found aa substitutions at six positions within the RBD region that are directly involved in binding with ACE-2 receptor (Wang et al., 2020; Yuan et al., 2020) including N439K (Scotland, Romania), L455F (England), A475V (USA, Australia), and F456L, Q493L and N501Y (USA) (Data S2).
Pan-India novel coronavirus SARS-CoV-2 genomics and global diversity analysis in spike protein.
Machine Learning Reveals the Critical Interactions for SARS-CoV-2 Spike Protein Binding to ACE2.
PMID: 34086459
2021
The journal of physical chemistry letters
Introduction: In agreement, experiments also demonstrate that both the L455Y point mutation and the F456L point mutation significantly diminish binding of the SARS-CoV-2 RBD to ACE2 by at least 75%.
Table: F456L
Insilico study on the effect of SARS-CoV-2 RBD hotspot mutants' interaction with ACE2 to understand the binding affinity and stability.
Molecular Dynamics Studies on the Structural Characteristics for the Stability Prediction of SARS-CoV-2.
PMID: 34445414
2021
International journal of molecular sciences
Abstract: In this study, Korean mutants for spike protein (D614G and D614A-C terminal domain, L455F and F456L-RBD, and Q787H-S2 domain) were investigated in patients.
Discussion: L455F and F456L are located in the RBD region, which interacts with ACE2.
Discussion: KDCA investigated Discussion: The other mutants:D614A, L455F, F456L, and Q787H:show more stability than the wild type in some complexes and are more unstable than the wild type in other situations.
Crucial Mutations of Spike Protein on SARS-CoV-2 Evolved to Variant Strains Escaping Neutralization of Convalescent Plasmas and RBD-Specific Monoclonal Antibodies.
Figure: Eight mutations (Y453F, L455F, F456L, A475V, A475S, T500S, N501Y, and Y505H) were in the RBD and hACE2 interaction region (RBD/hACE2); 10 mutations (V367I, V382L, R408G, N438K, L452Q, S477N, T478K, E484Q, S494P, and A520S) were in the RBD region but no
Molecular rationale for SARS-CoV-2 spike circulating mutations able to escape bamlanivimab and etesevimab monoclonal antibodies.
Result: The actual computational data for mutating these four viral protein residues into the SARS-CoV-2 circulating variants (E406D/Q, L455F/S/V, F456L/Y and Y505F/H/W) account for neutral-to-mildly negative effects on the stability of the corresponding S-RBDCoV-2/LY-CoV016 mAb binding interface, with estimated DeltaDeltaG values all below 1 kcal/mol for all alternative amino acids considered.
Result: The same data survey reported by Starr and coworkers led us to identify the following naturally occurring mutations at the SARS-CoV-2 spike protein residues contacting the LY-CoV016 Ab: E406D/Q, T415A/I/N/P/S, PMID: 34649620
2021
Genome medicine
Result: For example, alanine scanning revealed that the F456A mutation caused loss of binding of VH3-53/3-66 NAbs, but the natural F456L variation did not result in resistance to VH3-53/3-66 NAbs.
Prediction of the Effects of Variants and Differential Expression of Key Host Genes ACE2, TMPRSS2, and FURIN in SARS-CoV-2 Pathogenesis: An In Silico Approach.
PMID: 34720581
2021
Bioinformatics and biology insights
Result: We also analyzed the effect of 27 missense variants of SARS-CoV-2 spike protein (RBD) on the binding interaction of spike protein with ACE2 and observed that L452Q, T478K, L455F, F456L, S459F, A475V, N439K, L452R, T470N, E484D, E484A, E484K, E484Q, F486L, S494P, S494L, N501T,
ViMRT
SARS_CoV_2 mutation literature information.
PMID: 
2021
Transboundary and emerging diseases
