SARS_CoV_2 mutation literature information.


  A Simple RT-PCR Melting temperature Assay to Rapidly Screen for Widely Circulating SARS-CoV-2 Variants.
 PMID: 33758892       2021       medRxiv
Abstract: METHODS: RT-PCR primers and four sloppy molecular beacon (SMB) probes were designed to amplify and detect the SARS-CoV-2 N501Y (A23063T) and E484K (G23012A) mutations and their corresponding wild typ
Discussion: In designing this assay, we took advantage of the fact that the N501Y mutation is common to the three major SARS-CoV-2 variants of concern.
Discussion: Thus, this assay has the potential for relatively inexpensive high throughput testing for rapid identification of N501Y variants.


  Transmission, infectivity, and antibody neutralization of an emerging SARS-CoV-2 variant in California carrying a L452R spike protein mutation.
 PMID: 33758899       2021       medRxiv
Method: SARS-CoV-2 spike mutants (D614G, D614G+W152C, D614G+L452R, and D614G+N501Y) were cloned using standard site-directed mutagenesis and PCR.
Discussion: Notably, our findings reveal that the infectivity of L452R pseudoviruses was higher than D614G, but slightly reduced compared to that of N501Y pseudoviruses in 293T cells and human airway lung organoids.
Discussion: Thus, whether the L452R-carrying B.1.427/B.1.429 will continue to remain the predominant circulating strain in California, or whether it will eventually be replaced by the N501Y and E484K substitutions in the spike protein.
 PMID: 33774075       2021       Journal of virological methods
Abstract: N501Y was found in 206 (27.4 %) of the samples: 94 (28.2 %) men and 112 (26.85 %) women (p = 0.73).
Abstract: In order to discriminate N501Y variants quickly, a single nucleotide polymorphism (SNP) discrimination assay was designed and validated.
Abstract: The N501Y mutation in SARS-CoV-2 variants found in several strains from the UK, South Africa and Brazil has been linked to increased transmission.


  Mutational analysis of structural proteins of SARS-CoV-2.
 PMID: 33778179       2021       Heliyon
Method: Three separate structures of RBD with a point mutation, each namely S477N, V483A, and N501Y were created.
Result: Another was in the case of the docked structure of N501Y-RBD: ACE-2 interaction, T500 of S protein failed to form H bond with Y41 of ACE-2 and showed only hydrophobic interaction.
Result: Further, Q498 (S) generated an additional hydrophobic interaction with L45 (ACE-2) in the docked structure of N501Y-RBD: ACE


  SARS-CoV-2 spike variants exhibit differential infectivity and neutralization resistance to convalescent or post-vaccination sera.
 PMID: 33789085       2021       Cell host & microbe
Introduction: Additional mutations in spike, three amino acid deletions and seven missense mutations, including N501Y in RBD, make B.1.1.7 more infectious than the wild-type or the D614G strain.
Introduction: Both wild-type and the UK-N501Y pseudoviruses were efficiently neutralized by tested sera.
Introduction: Early reports have indicated that while the N501Y 


  Characterisation of B.1.1.7 and Pangolin coronavirus spike provides insights on the evolutionary trajectory of SARS-CoV-2.
 PMID: 33791702       2021       bioRxiv
Introduction: The spike mutations observed in current variants can be broadly divided into three categories based on their locations: N-terminal domain (NTD) mutations including deletions found in both B.1.1.7 and B.1.351; receptor binding domain (RBD) mutations including N501Y (B.1.1.7, B.1.351 and P.1) and E484K (B.1.351 and P.1); and stalk/S2 mutations including P681H proximal to the polybasic S1/S2 cleavage site (B.1.1.7).
Discussion: Thus far, studies have focussed on the contribution made by RBD mutations, and with good reason; N501Y and E484K have been implicated in increased ACE2 affinity and escape from anti- PMID: 33791722       2021       medRxiv
Result: Three of the analyzed sequences showed the aminoacid changes T183I, A890D, I1412T, P323L, L493F, N501Y, T553I, A570D, D614G, P681H, T716I, S982A, D1118H, Q27, R52I, Y73C, D3L, R203K, G204R and S235F placing them in the B.1.1.7 lineage.


  Infection- and vaccine-induced antibody binding and neutralization of the B.1.351 SARS-CoV-2 variant.
 PMID: 33798491       2021       Cell host & microbe
Introduction: The B.1.351 RBD contains three mutations (K417N, E484K and N501Y) which reduces antibody binding.
Introduction: The B.1.351 viral variant contains the following amino acid mutations within the viral spike protein: L18F, D80A, D215G, deletion at positions 242-244 (L242del, A243del, and L244del), K417N, E484K, N501Y, and D614G.
Introduction: The emerging B.1.351 SARS-CoV-2 variant includes three mutations within the receptor-binding domain (


  Structure-Function Analyses of New SARS-CoV-2 Variants B.1.1.7, B.1.351 and B.1.1.28.1: Clinical, Diagnostic, Therapeutic and Public Health Implications.
 PMID: 33803400       2021       Viruses
Abstract: While the N501Y mutation was observed in all three lineages, the 501Y.V1 and P.1 accumulated a different set of mutations in the Conclusion: As shown here, the N501Y mutation in all three variants may enhance ACE2 affinity but might not confer antibody resistance individually or neutralizing effects by convalescent plasma and vaccine sera.
Conclusion: The N501Y mutation, in particular, leads to stronger interaction with human ACE2 compared to its wildtype, although other co-occurring mutations along with N501Y might have a different overall effect.


  SARS-CoV-2 Variant of Concern 202012/01 Has about Twofold Replicative Advantage and Acquires Concerning Mutations.
 PMID: 33804556       2021       Viruses
Discussion: Importantly, the L18F mutation has also expanded in the South African strain 501Y.V2 defined by three spike mutations K417N, E484K, N501Y (thus sharing with the VOC strain spike mutation N501Y).
Discussion: In Brazil, in strain P.1 defined by three spike mutations K417T, E484K, N501Y (differing from the South African strain 501Y.V2 by substitution <
Discussion: In addition to double deletion 69-70HV, substitution N501Y in the RBD of spike is considered the most important VOC mutation.



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