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
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 infectivity, and many of them are believed to facilitate binding to ACE2.- Therefore, it is imperative to understand the mechanisms behind enhanced binding to ACE2 by SARS-CoV-2 RBD and how binding changes because of emerging mutations, notably K417N, E484
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.
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, RBD N501Y/K417N/E484K), in coating buffer (pH 9.6) overnight at 4 C, respectively.
Method: Recombinant SARS-CoV-2 ECD protein (Genscript, Cat no: Z03481) and the related RBD variants (RBD N5
Higher infectivity of the SARS-CoV-2 new variants is associated with K417N/T, E484K, and N501Y mutants: An insight from structural data.
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 ass
Figure: For RBD K417N vs WT, p = 0.0495; vs L452R, p = 0.0451; and vs E484K/K417N/N501Y, p = 0.0128.
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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