literature

SARS_CoV_2 mutation literature information.

Rational optimization of a human neutralizing antibody of SARS-CoV-2.

PMID: 34147856 2021 Computers in biology and medicine

Result: Comparatively, the mutation energies of E484K, E484K/N501Y and K417N/E484K/N501Y binding with H:V106R/H:P107Y are smaller than WT P2B-2F6.

Result: Some SARS-CoV-2 variants possess combination mutations such as E484K/N501Y and K417N/E484K/N501Y.

Table: K417N/E

Epitope Classification and RBD Binding Properties of Neutralizing Antibodies Against SARS-CoV-2 Variants of Concern.

PMID: 34149735 2021 Frontiers in immunology

Result: Thus, C1 NAb epitopes are predicted to be sensitive to K417N/T, Y453F, L455F, A475V, F486L,

Discussion: The current VoC include B.1.1.7-UK (N501Y, S494P*, E484K*), P.1-Japan/Brazil (K417N/T, E484K, N501Y), B.1.351-South Africa (K417N, E484K, N501Y) B.1.427/B.1.429-California (L452R), where amino acid changes in the SARS-CoV-2 S RBD of these VoC are listed in parentheses.

Preliminary Structural Data Revealed That the SARS-CoV-2 B.1.617 Variant's RBD Binds to ACE2 Receptor Stronger Than the Wild Type to Enhance the Infectivity.

PMID: 34160124 2021 Chembiochem

Introduction: These mutations in this strain may enhance virus transmissibility and infectivity, including the deletion of residues 69-70 and 144 and the substitution of A570D, D614G, T716I, S982A, D1118H, P681H, K417N, K417T, E484 K and N501Y.

Allosteric Cross-Talk among Spike's Receptor-Binding Domain Mutations of the SARS-CoV-2 South African Variant Triggers an Effective Hijacking of Human Cell Receptor.

PMID: 34161095 2021 The journal of physical chemistry letters

Introduction: As a result, we disclose that while N501Y (hallmark of the UK variant) enhances the binding affinity toward ACE2 and increases the alpha1-helix@ACE2 bending, the SA strain exploits a two-pronged strategy to more effectively infect the host cells by (i) increasing the allosteric signaling among the pivotal RBM loops, which acting as a tweezer more effectively grasp/bend alpha1-helix@ACE2 and (ii) hindering the interactions with class 1 and 2 mAbs (K417N and E484K, respectively) extracted from COVID-19 patients' sera (Figure 4 and Table S6).

Introduction: Hence, K417N and E484K substitutions alter the electrostatic complementarity between the RBD and class 1 and 2 mAbs, respectively (Figure 4 and Table S6),- impairing mAbs bindin

Recurrent emergence of SARS-CoV-2 spike deletion H69/V70 and its role in the Alpha variant B.1.1.7.

PMID: 34166617 2021 Cell reports

Method: The mutations (Delta69/70, Delta144, N501Y, A570D, D614G, P681H, S982A, T716I and D1118H or K417N, E484K and N501Y) were introduced by amplification with primers with similar Tm.

Analysis of SARS-CoV-2 variant mutations reveals neutralization escape mechanisms and the ability to use ACE2 receptors from additional species.

PMID: 34166623 2021 Immunity

Introduction: B.1.351 and P.1 each have three mutation sites in common within the RBD:

Method: P2C-1F11 Fab fragments were mixed with SARS-CoV-2 RBD containing K417N-E484K-N501Y mutations at a molar ratio of 1:1.2, incubated on ice for 2 h, and further purified by gel-filtration chromatography.

Method: The variant B.1.351 (GISAID: EPI_ISL_700450) was constructed with 10 mutations including L18F, D80A, D215G, 242-244del, S305T, K417N, E484K, N501Y, D614G and A701V.

COVID-19 mRNA vaccine induced antibody responses against three SARS-CoV-2 variants.

PMID: 34183681 2021 Nature communications

Result: The amino acid changes in the spike protein, especially the aforementioned E484K, K417N, and N501Y have recently been reported to affect the neutralizing efficacy of the antibodies.

Result: The three B.1.351 variant substitutions E484K, K417N, and N501Y are in the groove of the RBD-ACE2 interaction domain.

Discussion: The critical amino acid changes linked to escape from humoral immunity in the B.1.351 variant appear to be K417N, E484K, and N501Y.

Evolution, correlation, structural impact and dynamics of emerging SARS-CoV-2 variants.

PMID: 34188776 2021 Computational and structural biotechnology journal

Abstract: However, reported greater binding affinity of N501Y Spike with ACE2 does not seem to be entirely due to increased hydrophobic interactions, given that Spike mutation R417T in P.1 or K417N in B.1.351 results in the loss of a salt-bridge interaction between ACE2 and S-RBD.

Immune Evasion of SARS-CoV-2 Emerging Variants: What Have We Learnt So Far?

PMID: 34206453 2021 Viruses

Introduction: K417N was shown to be crucial to viral escape, effectively abrogating neutralization by some of the most common and potent neutralizing antibodies to SARS-CoV-2.

Introduction: However, a combination of K417N and N501Y was shown to enhance the binding with ACE2 and reduce binding with antibodies.

Introduction: The resistance to antibody neutralization of the B.1.351 variant is mainly ascribed to three mutations within RBD (K417N, E484K, N501Y).

Anti-SARS-CoV-2 Vaccines and Monoclonal Antibodies Facing Viral Variants.

PMID: 34207378 2021 Viruses

Introduction: It is characterized by three main mutations in the SARS-CoV-2 Spike protein: E484K co

Introduction: analyzed the impact of the neutralization of several mAbs on a panel of variants, including an authentic chimeric variant named Wash SA B.13 51, which contains the 20H/501Y.V2 Spike gene with other additional mutations (D80A, 242-244 del, R246I, K417N, E484K, N501Y, D614G and A701V), in addition to a panel of isogenic recombinant mutant variants (69-70 Del, K417N, E484K, N501Y, and/or D614G).

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