SARS_CoV_2 mutation literature information.


  Evidence of escape of SARS-CoV-2 variant B.1.351 from natural and vaccine-induced sera.
 PMID: 33730597       2021       Cell
Abstract: The receptor-binding domain mutations provide tighter ACE2 binding and widespread escape from monoclonal antibody neutralization largely driven by E484K, although K417N and N501Y act together against some important antibody classes.
Introduction: All three recently identified variant SARS-CoV-2 strains have acquired mutations in the ACE2 interaction surface of the RBD: N501Y in B.1.1.7; K417N, E484K, and N501Y in B.1.351; and K417T, E484K, and N501Y in P.1.
Discussion: Interestingly, repeated use of plasma therapy in an immunocompromised individual led to the transient emergence of the <


  SARS-CoV-2 501Y.V2 variants lack higher infectivity but do have immune escape.
 PMID: 33735608       2021       Cell
Introduction: Compared against the S protein of the 614G virus shows that 501Y.V2-3's S protein c
Table: N501Y
Discussion: The lethal variant is characterized by the superposition of two RBD mutations, Q493H and K417N, in the N501Y mutant background.


  Multiple SARS-CoV-2 variants escape neutralization by vaccine-induced humoral immunity.
 PMID: 33743213       2021       Cell
Result: A pseudovirus bearing only the three RBD mutations (K417N, E484K, and N501Y) largely, but not entirely, recapitulated the escape phenotype (Figures 5B and 5D).
Result: Despite this escape, antibodiesexhibited reduced, but detectable, binding to mutant RBD protein harboring B.1.351 mutations (K417N, E484K, and N501Y) by ELISA, which correlated with K417N+E484K+N501Y pseudovirus neutralization (R2 = 0.67, p < 0.0001) (Figure 5E).
Result: Similarly, neutralizing antibody responses were also significantly decreased for the Brazilian/Japanese P.1 strain (6.7-fold for BNT162b2, p < 0.0001; 4.5-


  Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera.
 PMID: 33743891       2021       Cell
Abstract: Variant B.1.1.7, now dominant in the UK, with increased transmission, harbors 9 amino acid changes in the spike, including N501Y in the ACE2 interacting surface.
Abstract: We map the impact of N501Y by structure/function analysis of a large panel of well-characterized monoclonal antibodies.


  Emergence in southern France of a new SARS-CoV-2 variant harbouring both N501Y and E484K substitutions in the spike protein.
 PMID: 33755190       2021       Journal of cellular physiology
Abstract: Herein, using structural and biophysical approaches, we explored that the specific mutations in the UK (N501Y), South African (K417N-E484K-N501Y), Brazilian (K417T-E484K-N501Y), and hypothetical (N501Y-E484K) variants alter the binding affinity, create new inter-protein contacts and changes the internal structural dynamics thereby increases the binding and eventually the infectivity.
Abstract: Our investigation highlighted that the South African (K417N-E484K-N501Y), Brazilian (K417T-E484K-


  Pan-India novel coronavirus SARS-CoV-2 genomics and global diversity analysis in spike protein.
 PMID: 33758785       2021       Heliyon
Table: N501Y
Discussion: Recently, the emergent UK variant strain named as VUI-202012/01 with defined as a set of 17 mutations, more significant N501Y was also observed and reported in India.


  Emergence in southern France of a new SARS-CoV-2 variant harbouring both N501Y and E484K substitutions in the spike protein.
 PMID: 33758836       2021       bioRxiv
Discussion: Although mutations in other parts of the genome could also contribute to this transmission phenotype, the N501Y substitution in the spike protein in particular appears to be a major determinant of efficient transmission.
Discussion: Combined with our data indicating that none except Delta69-70 and N501Y has a consistent phenotype, and some even show reduced fitness in our experimental results at certain timepoints, this suggests many if not all of the remaining mutations were not directly selected; these mutations probably occurred through drift mechanisms such as founder and hitchhiking effects, followed by maintenance via linkage to Delta69-70 and N501Y, or possibly via recombination, which occurs frequently during SARS-CoV-2 replication.
Discussion: Fortunately, tests to date with N501Y substitut


  Elicitation of broadly protective sarbecovirus immunity by receptor-binding domain nanoparticle vaccines.
 PMID: 33758839       2021       bioRxiv
Introduction: Although we did not observe any reduction in neutralization titers towards the B.1.1.7 variant, similar to what was seen with the N501Y point mutant, animals vaccinated with RBD-NP or HexaPro had 5-fold reduced serum neutralizing Ab titers against the B.1.351 S variant using HIV pseudovirus (GMT 1x102.
Introduction: The N501Y substitution present in the B.1.1.7 and B.1.351 lineages, the mink-associated Y453F substitution, and the prevalent N439K mutation did no
Method: The SARS-CoV-2-B.1.351-RBD-Avi was synthesized by GenScript into CMVR with K417N, E484K, and N501Y mutations from the Wuhan-1 strain used in the SARS-CoV-2-RBD-Avi construct listed above.


  Recombinant SARS-CoV-2 genomes are currently circulating at low levels.
 PMID: 33758853       2021       bioRxiv
Abstract: Recombinant genomes were also found to contain substitutions of concern for elevated transmissibility and lower vaccine efficacy, including D614G, N501Y, E484K, and L452R.
Result: Notably, two N501Y recombinant genotypes appear to be spreading, having been sampled multiple times in South Africa and in multiple provinces in Belgium.
Result: These putative recombinants include 847 genomes that harbor the D614G substitution, 8 with N501Y, and 5 with E484K.


  The plasmablast response to SARS-CoV-2 mRNA vaccination is dominated by non-neutralizing antibodies and targets both the NTD and the RBD.
 PMID: 33758878       2021       medRxiv
Result: Interestingly, almost all sera bound better to N501Y RBD (B.1.1.7) than to wild type (average 129% compared to wild type).
Result: Specifically, N501Y and Y453F combined with N439K increased affinity for human ACE2 by 5-fold (Figure 4, Suppl.
Result: Using biolayer interferometry (BLI), we measured rates of association and dissociation of the N501Y RBD mutant (B.1.1.7 carries that mutation as its sole RBD mutation), Y453F as found in mink isolates, N439K which is found in some European clades, a combination of Y453F and N439K,



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