A rigorous framework for detecting SARS-CoV-2 spike protein mutational ensemble from genomic and structural features.
PMID: 34806033
2021
Current research in structural biology
Result: Further, for the characteristic RBD mutations across VoCs (K417 T/N, L452R, S477N, T478K, E484K, and N501Y), we observed MTR scores between 0.68 and 0.91, suggesting these substitutions to be tolerant.
Result: Interestingly, five out of eight mutations of RBD are present in the epitope region, where L452Rand N501Y substitutions map to the RBD-loop epitope and S477N, T478K, and E484K are harboured in the RBD-ridge epitope.
Discussion: studied the effect of five prevalent
Booster of mRNA-1273 Strengthens SARS-CoV-2 Omicron Neutralization.
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.
Genome Sequencing Reveals a Mixed Picture of SARS-CoV-2 Variant of Concern Circulation in Eastern Uttar Pradesh, India.
Result: We also identified 8 substitution mutants in the SARS-CoV-2, K417N, G446V, L452R, S477N, T478K, E484Q, F490S, and A522V in the RNA binding domain (RBD) of S1 subunit of Spike protein.
Table: S477N
SARS-CoV-2 Omicron neutralization by therapeutic antibodies, convalescent sera, and post-mRNA vaccine booster.
Introduction: The predominant strain of Omicron has mutations in the spike gene encoding 15 amino acid changes in the receptor binding domain (RBD) of the spike surface protein (G339D, S371L, S373P, S375F, K417N, N440K, G446S, S477N, T478K, E484A, Q493R, G496S, Q498R, N501Y, and Y505H).
Prediction of SARS-CoV-2 Variant Lineages Using the S1-Encoding Region Sequence Obtained by PacBio Single-Molecule Real-Time Sequencing.
Result: All the missed mutations were due to a lack of coverage (<10 reads) and were grouped on the same amplicon NC_045512.2:22903-23122 (missing mutations: N440K, S477N, T478K, E484K, N501Y, A522S).
Result: For example, a variant harboring mutations S477N and D614G was identified as belonging to lineage B.1.160.
Result: Taken together, the most frequently missed mutations were G142D (n = 11), E156G, 157del, 158del (n = 6), N501Y (n = 6), S477N (n = 5), T95I
Insights into the Binding of Receptor-Binding Domain (RBD) of SARS-CoV-2 Wild Type and B.1.620 Variant with hACE2 Using Molecular Docking and Simulation Approaches.
Abstract: Recently, a new variant, B.1620, with mutations (S477N-E484K) in the spike protein's receptor-binding domain (RBD) has been reported in Europe.
Abstract: The current findings based on protein complex modeling and bio-simulation methods revealed the atomic features of the B.1.620 variant harboring S477N and E484K mutations in the RBD and the basis for infectivity.
Introduction: A report published in Cell reported that these mutations (S477N-E484K) in the RBD increase the binding affinity for the host receptor ACE2.
Introduction: Recently, a new variant, B.1620, with mutations (S477N
The Development of SARS-CoV-2 Variants: The Gene Makes the Disease.
PMID: 34940505
2021
Journal of developmental biology
Introduction: Mutation Y453F, along with N439K, G446V, K444E, and S477N, among others, which are located at the interface between the S1 and ACE2, have been shown to partially interfere with antibody binding and neutralization.
Additional Positive Electric Residues in the Crucial Spike Glycoprotein S Regions of the New SARS-CoV-2 Variants.
Phylogenomics and population genomics of SARS-CoV-2 in Mexico during the pre-vaccination stage reveals variants of interest B.1.1.28.4 and B.1.1.222 or B.1.1.519 and the nucleocapsid mutation S194L associated with symptoms.
Method: We marked the important mutations S477N, T478K, E484K, D614G, P681H/R and T732A.
Result: A similar scenario with multiple combinations at the c
Discussion: Mutations T478K and S477N, involving changes from similar hydroxylated side-chains (T and S) into positively charged basic amino acids (K and N), may have analogous functional roles, reinforcing the ability of the virus to bind to the human ACE2 receptor.
Discussion: The first one is in the flexible loop of the RBD, and includes S477N, T478K and E484K.