Conclusion: In addition, we investigated IFIE and binding energy between the ACE2 and the mutant N501Y on the SARS-CoV-2 S-protein regarding the mutation in common of the variants between the United Kingdom and South Africa, and our results can explain the high infectivity of the mutant.
Result: Along with these attractive interactions, it was confirmed that the binding energy including both statistical correction and desolvation (SC+Desolv) of the ACE2 with the mutant S-protein (N501Y) was further strengthened by ca.
Result: Currently, the highly transmissible variants of the United Kingdom
Result: analyzed the complex between the SARS-CoV-2 S-protein of the N501Y variant and a neutralizing antibody by cryo-electron microscopy (not yet published at February 7, 2021).
Thermodynamics and kinetics in antibody resistance of the 501Y.V2 SARS-CoV-2 variant.
Abstract: Three substitutions in the RBD including K417N, E484K, and N501Y alter the free energy landscape, binding pose, binding free energy, binding kinetics, hydrogen bonding, nonbonded contacts, and unbinding pathway of RBD + NAb complexes.
Adaptation of SARS-CoV-2 in BALB/c mice for testing vaccine efficacy.
Result: In the mutants, other amino acids were substituted at certain locations; for example, A23063T indicates that alanine at position 23063 was replaced by threonine.) Structural remodeling also suggested that the N501Y substitution in the RBD of SARS-CoV S protein increased the binding affinity of the protein to mouse ACE2.
Result: The A23063T mutation resulted in a Discussion: The N501Y mutation seems to provide a more favorable interaction with mouse ACE2 for docking and entry, thus leading to the increased virulence phenotype in mice.
Discussion: Whether the other three mutations, except for N501Y, also regulated viral infectivity remains to be determined.
An engineered decoy receptor for SARS-CoV-2 broadly binds protein S sequence variants.
Abstract: Variant N501Y in the RBD, which has emerged in a rapidly spreading lineage (B.1.1.7) in England, enhances affinity for wild type ACE2 20-fold but remains tightly bound to engineered sACE22.v2.4.
Result: After titrating the concentrations of 8his-tagged sACE22(WT) and sACE22.v2.4 and measuring bound protein to S-expressing cells by flow cytometry, it was found S-N501W and S-N501Y do show enhanced specificity for wild type sACE22, but the effect is small and sACE22.v2.4 remains the stronger binder (Figure 5C).
Result: Both N501W and N501Y mutants of SARS-CoV-2 RBD displayed increased affinity for wild type ACE2 and engineered
Neutralising antibodies in Spike mediated SARS-CoV-2 adaptation.
Abstract: Although little change was observed in the overall viral population structure following two courses of remdesivir over the first 57 days, N501Y in Spike was transiently detected at day 55 and V157L in RdRp emerged.
Result: Notably, spike variant N501Y, which can increase the ACE2 receptor affinity, and which is present in the new UK B1.1.7 lineage, was observed on day 55 at 33% frequency, but was eliminated by the sweep of the NSP2/RdRp variant.
SARS_CoV_2 mutation literature information.
PMID: 
2021
Chemical science
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