SARS-CoV-2 testing and sequencing for international arrivals reveals significant cross border transmission of high risk variants into the United Kingdom.
Introduction: Indeed, evidence suggests both the Moderna and Pfizer vaccines are less effective at neutralising viruses with these mutations and of 17 vaccine-elicited antibodies tested, 9 were at least 10 times less effective against pseudotyped viruses containing E484K, 5 against K417N and 4 against N501Y.
Introduction: K417 has been found to be 60-100% buried in class 1 antibody paratopes and K417N has also been shown to significantly reduce sera neutralisation.
Introduction: The combination of nearby RBD mutations K417N/T, E484K and N501Y found in B.1.351 (South Africa) and P.1 (Brazil) make these particularly concerning variants.
A Simple Reverse Transcriptase PCR Melting-Temperature Assay To Rapidly Screen for Widely Circulating SARS-CoV-2 Variants.
PMID: 34288729
2021
Journal of clinical microbiology
Introduction: All three variants, B.1.1.7, B.1.351, and P.1, contain the N501Y mutation, while the South African and Brazilian variants additionally contain mutations in E484K and K417N.
Neutralization of SARS-CoV-2 by highly potent, hyperthermostable, and mutation-tolerant nanobodies.
Abstract: We constructed nanobody tandems and identified nanobody monomers that tolerate the K417N/T, E484K, N501Y, and L452R immune-escape mutations found in the Alpha, Beta, Gamma, Epsilon, Iota, and Delta/Kappa lineages.
Mutational analysis in international isolates and drug repurposing against SARS-CoV-2 spike protein: molecular docking and simulation approach.
Method: The B.1.351 Spike carries the mutations D80A, D215G, del242-244, K417N, E484K, N501Y, D614G, an
Discussion: B.1.351 and P.1 have in common three RBD substitutions (K417N/T, E484K and N501Y) whereas B.1.351, P.1 and B.1.1.7 contain the N501Y substitution.
Discussion: Furthermore, three major classes of neutralizing antibodies (RBS-A, -B, and -C) identified from convalescent patients are sensitive to either the K417N (RBS-A) or E484K (RBS-B and -C) substitutions present in B.1.351.
Structural and functional basis for pan-CoV fusion inhibitors against SARS-CoV-2 and its variants with preclinical evaluation.
PMID: 34326308
2021
Signal transduction and targeted therapy
Introduction: Indeed, under the pressure of host immunity, some mutations, which have occurred in the RBD, such as N501Y, K417N, and E484K, are found in numerous variants, including B.1.1.248 and B.1.351 dominant variants.
Result: Moreover, variants with combinational mutations in S protein, including Result: To explore whether EK1 peptides are antivirally active against infection mediated by spike protein carrying these mutations, we assessed their antiviral efficacy on infection by pseudoviruses (PsVs) with K417N, E484K, N501Y or D614G single mutation in their S proteins.
The challenge of screening SARS-CoV-2 variants of concern with RT-qPCR: One variant can hide another.
PMID: 34332998
2021
Journal of virological methods
Abstract: From week 18 we used in addition the new NovaplexSARS-CoV-2 Variants II Assay for samples with no targets found with the Variants I assay or with the mutation E484K alone, in order to screen the mutations L452R, K417N/T
Discussion: It distinguishes the VOC B.1.351 from the VOC P.1 by amplification of the K417N and K417T mutations respectively when both the N501Y and E484K mutations were found positive with the Variant I Assay.
Discussion: Since early May 2021, a new NovaplexSARS-CoV-2 Variants II Assay has been available on the market to detect L452R, K417N, K417T and W152C mutations.
Binding affinity and mechanisms of SARS-CoV-2 variants.
PMID: 34336146
2021
Computational and structural biotechnology journal
Introduction: 1(a), the 501Y.V1 variant contains N501Y mutation in the RBD, the 501Y.V2 variant contains the mutations of K417N, E484K, and N501Y in the RBD, and the N439K variant contains the mutation of N439K in the RBD.
Introduction: Introduction: However, the 501Y.V1 variant had a stronger binding affinity to hACE2 than the 501Y.V2 variant, suggesting that the K417N and E484K mutations in the 501Y.V2 variant weaken the binding affinity between the SARS-CoV-2 RBD and hACE2 compared to the 501Y.V1 variant by breaking hydrogen bonds.
Conformational Variability Correlation Prediction of Transmissibility and Neutralization Escape Ability for Multiple Mutation SARS-CoV-2 Strains using SSSCPreds.
Introduction: K417N/T mutations of Beta and Gamma appear to make the RBD-ACE2 interactions less strong compared to Alpha variant.
Introduction: K417N.
Introduction: As shown in Figure 2B,C, Alpha and Beta variants include N501Y mutation, while Beta variant involves two additional mutations, K417N and E484K.
Introduction: They investigated each specific mutation, N501Y, K417N/T, and E484K, and reported that F486, Q498, T500, and Y505 in RBD are important residues across viral variants in the RBD-ACE2 interface.
Introduction: To gain molecular insight into the differe
SARS_CoV_2 mutation literature information.
PMID: 
2021
EClinicalMedicine
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