literature

SARS_CoV_2 mutation literature information.

Allosteric Determinants of the SARS-CoV-2 Spike Protein Binding with Nanobodies: Examining Mechanisms of Mutational Escape and Sensitivity of the Omicron Variant.

PMID: 35216287 2022 International journal of molecular sciences

Result: We also examined the effect of Omicron mutations in the RBD (G339D, S371L, S373P, S375F, K417N, N440K, G446S, S477N, T478K, E484A, Q493R, G496S, Q498R, N501Y, Y505H) on binding of Nb6, VHH E, and VHH E/VHH V nanobodies (Figure 7).

SARS-CoV-2 Omicron variant: Immune escape and vaccine development.

PMID: 35317190 2022 MedComm

Introduction: In addition, SARS-CoV-2 variants (e.g., Omicron) with N440K mutation are also more likely to escape antibody neutralization activities.

Introduction: Specifically, BA.1 and BA.2 display 20 identical spike mutations, which are G339D, S373P, S375F, K417N, N440K, S477N, T478K, E484A, Q493R, Q498R, N501Y, Y505H, D614G, H655Y, N679K, P681H,

PMID: 35312321 2022 Journal of chemical information and modeling

Method: The omicron variant has 15 mutations in the RBD domain of the S protein: G339D, S371L, S373P, S375F, K417N, N440K, G446S, S477N, T478K, E484A, Q493K/R, G496S, Q498R, N501Y, and Y505H.

Result: In the crystal structure, S375F, N440K,

Table: N440K

Cross-Neutralizing Breadth and Longevity Against SARS-CoV-2 Variants After Infections.

PMID: 35281007 2022 Frontiers in immunology

Introduction: Finally, B.1.1.529, which was detected in Botswana on November 11, 2021 and South Africa on November 14, 2021, has 15 mutations (G339D, S371L, S373P, S375F, K417N, N440K, G446S, S477N, T478K, E484A, Q493R, G496S, Q498R, N501Y, and Y505H) in the RBD.

SARS-CoV-2 Mutations and Their Impact on Diagnostics, Therapeutics and Vaccines.

PMID: 35273977 2022 Frontiers in medicine

Table: N440K

Omicron variant (B.1.1.529) of SARS-CoV-2: understanding mutations in the genome, S-glycoprotein, and antibody-binding regions.

PMID: 35258772 2022 GeroScience

Abstract: There are several mutations in the antibody-binding region including K417N, E484A, Q493K, Q498R, N501Y, and Y505H and several near the antibody-binding region (S477N, T478K, G496S, G446S, and N440K).

Abstract: Various new receptor-binding domain mutations were detected, including Q493K, G496S, Q498R, S477N, G466S, N440K, and Y505H.

Discussion: <

Human serum from SARS-CoV-2-vaccinated and COVID-19 patients shows reduced binding to the RBD of SARS-CoV-2 Omicron variant.

PMID: 35236358 2022 BMC medicine

Table: N440K

Rapidly Identifying New Coronavirus Mutations of Potential Concern in the Omicron Variant Using an Unsupervised Learning Strategy.

PMID: 35233566 2022 Research square

Abstract: To build an investigative framework, we have applied an unsupervised machine learning approach to 4296 Omicron viral genomes collected and deposited to GISAID as of December 14, 2021, and have identified a core haplotype of 28 polymutants (A67V, T95I, G339D, R346K, S371L, S373P, S375F, K417N, N440K, G446S, S477N, T478K, E484A, Q493R, G496S, Q498R, N501Y, Y505H,

SARS-CoV-2 Omicron Spike recognition by plasma from individuals receiving BNT162b2 mRNA vaccination with a 16-week interval between doses.

PMID: 35216664 2022 Cell reports

Discussion: Previous in vitro studies already showed the association of some of these mutations with increased infectivity, ACE2 interaction (N501Y, P681H), or immune evasion (K417N, N440K, G446S, S477N, E484A/K, Q493R).

Binding of Human ACE2 and RBD of Omicron Enhanced by Unique Interaction Patterns Among SARS-CoV-2 Variants of Concern.

PMID: 35118473 2022 bioRxiv

Method: In each variant, the Alpha includes N501Y mutation, Delta has L452R and T478K mutations, and Omicron contains 15 mutated amino acids, i.e., G339D, S371L, S373P, S375F, K417N, N440K, G446S, S477N, T478K, E484A, Q483K/R, G496S, Q498R, N501Y, and Y505H (see also Figures 1B and 2D).

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