Abstract: This resistance hierarchy corresponded with Y144del and 242-244del mutations in the N-terminal domain and K417N/T, E484K, and N501Y mutations in the receptor-binding domain (RBD) of SARS-CoV-2.
Introduction: B.1.351 and P.1 each have three mutation sites in common within the RBD:K417N/T, E484K, and N501Y:which may change their antigenic profile.
Discussion: Because K417N/T also markedly reduced binding to soluble ACE2, this mutation may shift the balance in favor of binding to an antibody rather than to ACE2.
Discussion: More importantly, P2C-1F11, which is currently in therapeutic development, w
Immune Evasion of SARS-CoV-2 Emerging Variants: What Have We Learnt So Far?
Introduction: Five mutations are located within NTD (L18F, T20N, P26S, D138Y, R190S), three in RBD (K417T, E484K, N501Y), two in the C-terminal domain of S1 and near the furin cleavage site (D614G, H655Y), and one in S2 (T1027I) (Figure 3).
Anti-SARS-CoV-2 Vaccines and Monoclonal Antibodies Facing Viral Variants.
Introduction: It presents mutations in common with the 20H/501Y.V2 variant located at the RBM of the S protein: N501Y and K417T, which may be involved in enhancing transmission, and E484K, which may be related to a slight improvement in receptor-binding affinity and immune escape (Table 1).
Use of Lateral Flow Immunoassay to Characterize SARS-CoV-2 RBD-Specific Antibodies and Their Ability to React with the UK, SA and BR P.1 Variant RBDs.
Abstract: The potential contributions of the mutations (N501Y, E484K, and K417N/T) contained in these variants' RBDs to the antibody pairing capability, neutralization activity, and therapeutic antibody targeting strategy are discussed.
Introduction: Figure 1 summarizes currently circulating SARS-CoV-2 variants and their respective mutations within the spike RBD, which include the following: N501Y in the UK, SA, and BR-P.1 variants; E484K/Q in the SA, BR P.1, BR P.2, NY, and IN variants; K417N/T in the SA and BR P.1 variants; L452R in the CA and IN variants; S477N in some NY variants
The emerging SARS-CoV-2 variants of concern.
PMID: 34211709
2021
Therapeutic advances in infectious disease
Discussion: However, the study further showed that variants that carry K417N/T, E484K, and N501Y mutations, such as the UK (B1.1.7/501Y.V1), South African (501Y.V2), and Brazil (B1.1.28/501.V3) variants, can reduce the neutralization potency of vaccine plasma.
Insilico study on the effect of SARS-CoV-2 RBD hotspot mutants' interaction with ACE2 to understand the binding affinity and stability.
Introduction: 20 J/501Y.V3) emerged in Brazil, contains mutations K417T, E484K and N501Y in the RBD with evidence to affect transmissibility and antigenic profile.
Antibody Cocktail Exhibits Broad Neutralization Activity Against SARS-CoV-2 and SARS-CoV-2 Variants.
Introduction: The recent emerging variants of concern observed in the United Kingdom (B.1.1.7 with mutations N501Y, A570D and del69/70), South Africa (B.1.351 with mutations K417N, E484K and N501Y), Brazil (P.1 and P.2 with mutations K417T, E484K and N501Y) (Long et al.) and India (B.1.617 with mutations L452R and E484Q) (Cherian et al.) initially respond more tightly to ACE2 and appear to be more infectious to human (Laffeber et al.; Tian et al.).
Discussion: Variants of concern observed in the United Kingdom (B.1.1.7 with mutations N501Y), South Africa (B.1.351 with mutations
A bivalent recombinant vaccine targeting the S1 protein induces neutralizing antibodies against both SARS-CoV-2 variants and wild-type of the virus.
Result: Based on D614G, other mutations existing in RBD are K417N/K417T, E484K, and N501Y which might affect the recognition and binding of SARS-CoV-2 to ACE2.
Genomic monitoring unveil the early detection of the SARS-CoV-2 B.1.351 (beta) variant (20H/501Y.V2) in Brazil.
Result: P.1 defining mutations related to each genomic region were the following: ORF1ab: S1188L, K1795Q, E5665D; spike: L18F, T20N, P26S, D138Y, R190S, K417T, E484K, N501Y, H655Y, T1027I; Orf8: E92K; and nucleocapsid: P80.
Potent and protective IGHV3-53/3-66 public antibodies and their shared escape mutant on the spike of SARS-CoV-2.
Method: Specifically, protein A (Sino Biological) was firstly covalently immobilized onto a CM5 sensor chip, followed by capture of the individual antibodies and then injection of purified soluble SARS-CoV-2 WT and K417R/A/E/N/T mutant RBDs at five different concentrations.
Result: K417A/E/N/T mutants resulted in complete resistance to P5A-3C8, P22A-1D1, and P5A-1D2 while remaining sensitive to P2C-1F11.
Result: K417A/E/N/T mutations disrupted these salt bridges, leading to loss of neutralizing activity.
Result: In contrast, K417A/E/N/T mutants substantially reduced binding by P22A-1D1 and P5A-1D2, while impact on P5A-3C8 and P2C-1F11 was relatively moderate.
SARS_CoV_2 mutation literature information.
PMID: 
2021
Immunity
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