Discussion: All 3 VOCs harbor an N501Y mutation within S-RBD, while the B.1.351 and P.1 variants contain 2 additional RBD changes, K417N/T and E484K.
Machine Learning Reveals the Critical Interactions for SARS-CoV-2 Spike Protein Binding to ACE2.
PMID: 34086459
2021
The journal of physical chemistry letters
Abstract: Lastly, the energetics of emerging SARS-CoV-2 mutations were studied, showing that the affinity of the RBD for ACE2 is increased by N501Y and E484K mutations but is slightly decreased by K417N.
Introduction: Although the K417N mutation was unfavorable for ACE2 binding, the effect was small (+0.4 kcal/mol) and could be compensated by decreased antibody binding.
Introduction: Finally, we considered the K417N mutation, found in the South African and Brazilian variants.
Introduction: However, K417N has been found in simulations to have an even more detrimental effect on monoclonal antibody binding.
Introduction: Recent mutations of SARS-CoV-2 have increased
Table: K417N
Nanobodies from camelid mice and llamas neutralize SARS-CoV-2 variants.
Introduction: A second variant of concern is B.1.351, which combines N501Y with two additional RBD substitutions (K417N and E484K).
Introduction: In contrast to their efficacy against the wild-type virus, Nb17, Nb19 and Nb56 were unable to neutralize viruses carrying the E484K substitution alone or in combination with K417N and N501Y.
Method: The mutants E484K and KEN (K417N, E484K and N501Y) were constructed in the context of a pSARS-CoV-2-SDelta19 variant with a substitution in the furin cleavage site (R683G).
Figure: Pseudotyped viruses containing
Characterization of SARS-CoV-2 different variants and related morbidity and mortality: a systematic review.
PMID: 34103090
2021
European journal of medical research
Table: K417N
Therapeutic effect of CT-P59 against SARS-CoV-2 South African variant.
PMID: 34119826
2021
Biochemical and biophysical research communications
Result: KD values of CT-P59 were reduced by approximately 2-, 2-, and 10-fold in E484K, N501Y, and triple mutant (K417N/E484K/N501Y), respectively (Table 1 ).
Result: The equilibrium dissociation constant (KD) of CT-P59 against K417N was equivalent to that against wild type.
Result: To assess the efficacy of CT-P59 against SA variant, we determined the binding affinity of CT-P59 against individual and triple mutant RBDs (K417N, E484K, N501Y, and K417N/E484K/N501Y), whic
Table: K417N
Potent RBD-specific neutralizing rabbit monoclonal antibodies recognize emerging SARS-CoV-2 variants elicited by DNA prime-protein boost vaccination.
Introduction: B.1.351 bears three RBD mutations (K417N, E484K, and N501Y), in addition to several mutations outside of RBD, leading to substantial or complete loss of neutralization potency from humoral immunity elicited by natural infection and vaccination.
Method: Briefly, 96-well microtiter plates (Corning, Cat no: 9018) were coated with 100 muL of 1 mug/mL ectodomain of spike protein (ECD), S1 protein, RBD protein, RBD variants protein (RBD E484K, RBD K417N, RBD N501Y,
RT-qPCR Assays for Rapid Detection of the N501Y, 69-70del, K417N, and E484K SARS-CoV-2 Mutations: A Screening Strategy to Identify Variants With Clinical Impact.
PMID: 34123874
2021
Frontiers in cellular and infection microbiology
Result: For example,
Figure: (A) Shows the alignment for the 69/70 deletion assay; (B) shows the alignment for the K417N mutation assay; (C) shows the alignment for the E484K/N501Y assay.
Figure: (A) The curves of four independent reactions are shown; the purple curves with a lower Cq value show the forward primer amplification directed to the sequence without K417N mutation (Reaction 1) in a sample of COVID-19 patients or control C+ without-Mut.
Figure: (B) The purple curves with a lower Cq value show the amplification of the forward primer directed to the K417N mutation (417N Fw) (Reaction 2) using synthetic control C+ Mut484-501-417 (which contains the mutation).
Figure: Amplification curves for the K417N assay.
Rapid Increase of SARS-CoV-2 Variant B.1.1.7 Detected in Sewage Samples from England between October 2020 and January 2021.
Introduction: Amino acid substitutions at residue 417, K417N in B.1.351 and K417T in P.1, appear to improve evasion from antibodies in combination with N501Y and E484K.
Introduction: B.1.351 and P.1 variants have two more spike mutations of biological significance: E484K and K417N/T, both located in the RBD and both important for ACE-2 binding and antibody recognition.
An ACE2 Triple Decoy that neutralizes SARS-CoV-2 shows enhanced affinity for virus variants.
Introduction: We therefore assessed the affinity of our ACE2 decoy, as compared to wild type (WT) ACE2, for S RBD with a variety of single or multiple mutations associated with the currently predominant variants, including the B.1.351 variant expressing E484K, K417N, and N501Y mutations, the B.1.1.7 variant (N501Y), and the B.1.427/B.1.429 L452R variant.
Result: 3s, inhibition in the surrogate virus neutralization assay modified to assess competition by the ACE2 Triple Decoy for ACE2 (WT) binding to S RBD was similar for S RBD WT, E484K,
Recent progress on the mutations of SARS-CoV-2 spike protein and suggestions for prevention and controlling of the pandemic.
PMID: 34146731
2021
Infection, genetics and evolution
Introduction: Compared with the spike protein of SARS-CoV-2 Wuhan-1 strain, the spike protein of 501Y V2-3 contains eight mutations: four mutations in NTD (L18F, D80A, D215G, and Delta242-244), three mutations in viral RBD (K417N, E484K, and Figure: Among these mutations, the most representative ones are substitution mutations such as D614G, N501Y, Y453F, N439K/R, P681H, K417N/T, and E484K, and deletion mutations of DeltaH69/V70 and Delta242-244.
SARS_CoV_2 mutation literature information.
PMID: 
2021
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