Introduction: According to the United States (US) Center for Disease Control (CDC), signature Spike mutations in the aggregated Delta and Delta Plus variant include T19R, (V70F*), T95I, G142D, E156-, F157-, R158G, (A222V*), (W258L*), (K417N*), L452R, T478K, D614G, P681R, and D950N.
Introduction: Hence, as noted above, the Delta Plus variant is not just a variant of Delta signified by the K417N mutation but has additional mutations that need to be considered.
Introduction: The B.1.1.7 variant, now labelled Alpha variant, carries the N501Y mutation in the S receptor-binding domain (RBD) whereas the B.1.351 variant, labelled Beta variant, has three notable mutations in the S RBD, namely, K417 N, E484K, and N501Y.
The Emergence and Spread of Novel SARS-CoV-2 Variants.
Abstract: Our analysis suggests that B.1.1.7, B.1.351, and P.1 are more easily spreading than other variants, and the key mutations of S protein, including N501Y, E484K, and K417N/T, have high mutant frequencies, which may have become the main genotypes for the spread of SARS-CoV-2.
Result: Although, K417N site does not combine with ACE2, it is an epitope of neutralizing antibody-like E484K, and so it may be selected to evade humoral immune reaction.
Result: So N501Y, E484K, and K417N/T may have become the main genotypes for the spread of SARS-CoV-2 and may change the structure, properties, and other characteristics of S pr
N439K Variant in Spike Protein Alter the Infection Efficiency and Antigenicity of SARS-CoV-2 Based on Molecular Dynamics Simulation.
PMID: 34414185
2021
Frontiers in cell and developmental biology
Discussion: Among the E484K, K417N, and N501Y mutations in the receptor-binding domain of Spike caused widespread escape from monoclonal antibodies.
N501Y mutation of spike protein in SARS-CoV-2 strengthens its binding to receptor ACE2.
Result: The mutation resulted in a slightly weaker or similar affinity to cell-surface ACE2, whereas the N501Y, K417N,
Discussion: Additional mutations within the receptor-binding site (K417N and E484K) changed the amino acid sequence of the epitope and may contribute to the escape from antibody binding.
Discussion: Indeed, the results from flow cytometry showed that E484K contributed less to the interaction increment than N501Y, whereas K417N even decreased the interaction.
Discussion: The effects of the E484K and K417N mutations may cancel each other out, and N501Y is the dominant site in affecting the interaction.
mRNA-1273 protects against SARS-CoV-2 beta infection in nonhuman primates.
Introduction: Acquisition of amino acid substitutions in the S RBD- namely K417N, E484K, and N501Y:and in the NTD, such as L18F, D80A, D215G, and Delta242-244, is associated with increased transmissibility and reduction in neutralization sensitivity.
The impact of spike N501Y mutation on neutralizing activity and RBD binding of SARS-CoV-2 convalescent serum.
Abstract: Enzyme immunoassay using 272 convalescent sera showed reduced binding of anti-RBD IgG to N501Y or Introduction: The B.1.351 and P.1 variants also contain mutation at the spike amino acid position 484 (E484K) and at position 417 (K417N for B.1.351; K417T for P.1).
Method: Recombinant RBD (amino acid residues 306-543) of SARS-CoV-2 spike protein from the reference sequence Wuhan-Hu-1 (GenBank ID YP_009724390.1) (wild type) or with the mutations N501Y or N501Y-E484K-K417N were expressed and purified as we described previously with modifications.
Key Interacting Residues between RBD of SARS-CoV-2 and ACE2 Receptor: Combination of Molecular Dynamics Simulation and Density Functional Calculation.
PMID: 34428371
2021
Journal of chemical information and modeling
Abstract: In the Beta variant, K417N reduces the binding, E484K slightly enhances it, and N501Y significantly increases it as in Alpha.
Introduction: The RBD with the Alpha variant contains a mutation of asparagine to tyrosine at position 501 (N501Y), while the Beta variant has two new mutations, K417N and E484K, in addition to N501Y.
Result: The K417N mutation in Beta reduces the binding due to loss of the salt-bridge between K417 (SARS2) and D30 of ACE2, while the E484K mutation (i.e., Group C) provides a slight increase in the binding via forming an ion pair with E75 of ACE2.
Epitope diversity of SARS-CoV-2 hyperimmune intravenous human immunoglobulins and neutralization of variants of concern.
Abstract: Significant reduction of hCoV-2IG binding was observed to RBD-E484K followed by RBD-N501Y (but not RBD-K417N).
Method: Antibody preparations were evaluated by SARS-CoV-2 pseudovirus neutralization assay (PsVNA) using WA-1 strain, UK variant (B.1.1.7 with spike mutations: H69-V70del, Y144del, N501Y, A570D, D614G, P681H, T716I, S982A, and D1118H), SA variant (B.1.351 strain with spike mutations PMID: 34433803
2021
Signal transduction and targeted therapy
SARS_CoV_2 mutation literature information.
PMID: 
2021
Journal of autoimmunity
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