literature

SARS_CoV_2 mutation literature information.

Multiple SARS-CoV-2 variants escape neutralization by vaccine-induced humoral immunity.

PMID: 33743213 2021 Cell

Introduction: This lineage bears three RBD mutations, K417N, E484K, and N501Y, in addition to several mutations outside of RBD, and several reports have suggested that convalescent and vaccinee sera have decreased cross-neutralization of B.1.351 lineage variants.

Introduction: We find that although neutralization is largely preserved against many variants, those containing the K417N/T, E484K, and N501Y RBD mutations, namely, P.1 and B.1.351 variants, have significantly decreased neutralization even in fully vaccinated individuals.

Result: A pseudovirus bearing only the three RBD mutations (

Higher infectivity of the SARS-CoV-2 new variants is associated with K417N/T, E484K, and N501Y mutants: An insight from structural data.

PMID: 33755190 2021 Journal of cellular physiology

Abstract: Herein, using structural and biophysical approaches, we explored that the specific mutations in the UK (

Table: K417N

Figure: (c) show the individual residue flexibility, that is, K417N, K417T, E48K, and N501Y.

Pan-India novel coronavirus SARS-CoV-2 genomics and global diversity analysis in spike protein.

PMID: 33758785 2021 Heliyon

Table: K417N

Elicitation of broadly protective sarbecovirus immunity by receptor-binding domain nanoparticle vaccines.

PMID: 33758839 2021 bioRxiv

Introduction: To assess the neutralization breadth of RBD-NP-elicited Abs, we evaluated serum neutralizing activity against a panel of pseudotyped viruses comprising wild-type (D614G) SARS-CoV-2 S and nine single-residue SARS-CoV-2 RBD mutants detected in clinical isolates (G446S, Y453F, L455F, T478I, E484A

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.

A Simple RT-PCR Melting temperature Assay to Rapidly Screen for Widely Circulating SARS-CoV-2 Variants.

PMID: 33758892 2021 medRxiv

Introduction: All three, B.1.1.7, B.1.352 and P.1 variants contain the N501Y mutation, while the South African and Brazilian variants additionally contain mutations in E484K and K417N.

Transmission, infectivity, and antibody neutralization of an emerging SARS-CoV-2 variant in California carrying a L452R spike protein mutation.

PMID: 33758899 2021 medRxiv

Introduction: The other two VOCs, B.1.351 detected in South Africa and P.1 first detected in Brazil, carry E484K and K417N/K417T in addition to N501Y mutations.

SARS-CoV-2 spike variants exhibit differential infectivity and neutralization resistance to convalescent or post-vaccination sera.

PMID: 33789085 2021 Cell host & microbe

Introduction: Effects of spike RBD mutations, N501Y, K417N, and E484K (or their combinations) on viral infectivity (i.e., transduction and inhibition of viral entry) were also documented.

Introduction: Finally, pseudoviruses with the K417N/E484K and the SA-N501Y/K417N/E484K spike mutations exhibited the highest neutralization resistance to post-vaccination sera, emphasizing the role of E484K mutation in neutralization resistance (Figure 2D).

Introduction: However, pseudovirus carrying the SA-N501Y/

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

Result: The 501Y.V2 and P.1 variants show a different set of mutations besides N501Y:E484K in both and K417N (in 501Y.V2) and K417T (in P.1).

Result: The N501Y, E484K, K417N/T mutations are localized near the ACE2 interaction interface but distant from C135/CR3022 binding sites (Figure S3A,B).

SARS-CoV-2 Variant of Concern 202012/01 Has about Twofold Replicative Advantage and Acquires Concerning Mutations.

PMID: 33804556 2021 Viruses

Result: The same mutation has occurred in the fast expanding South African and Brazilian (Manaus) strains that share with the VOC substitution N501Y and additionally have a mutation of residue 417: either K417N (South African strain 501Y.V2) or K417T (Manaus strain P.1).

Result: This mutation occurred independently in the South African strain 501Y.V2, where it is accompanied by two other mutations in spike RBD: K417N and E484K.

Discussion: Importantly, the L18F mutation has also expanded in the South African strain 501Y.V2 defined by three spike mutations K417N, E484K,

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