SARS_CoV_2 mutation literature information.


  An Epidemiological Analysis of SARS-CoV-2 Genomic Sequences from Different Regions of India.
 PMID: 34067745       2021       Viruses
Abstract: These sequences also revealed the presence of single independent mutations-E484Q and N440K-from Maharashtra (first observed in March 2020) and Southern Indian States (first observed in May 2020), respectively.
Discussion: Another immune escape mutation, the N440K amino acid in the spike protein, was also observed in Telangana (n = 7), Andhra Pradesh (n = 5), and Assam (n = 1) from May 2020.


  Mutation in a SARS-CoV-2 Haplotype from Sub-Antarctic Chile Reveals New Insights into the Spike's Dynamics.
 PMID: 34064904       2021       Viruses
Discussion: Whereas mutations emerging within the receptor binding domain such as N501Y and N440K might have a direct impact on ACE2 binding, our work further supports the idea that distant variations affecting RBD dynamics, such as D614G, must also be monitored.


  Insights on the mutational landscape of the SARS-CoV-2 Omicron variant.
 PMID: 34909771       2021       bioRxiv
Result: Our network analysis ranks Omicron mutations N440K, G446S, G496S, and Q498R as most likely to confer enhanced class 3 antibody escape based on these sites having the strongest network interactions with the antibodies surveyed.


  Structural Modeling of the SARS-CoV-2 Spike/Human ACE2 Complex Interface can Identify High-Affinity Variants Associated with Increased Transmissibility.
 PMID: 33992693       2021       Journal of molecular biology
Abstract: By focusing on natural variants at the Spike-hACE2 interface and assessing over 700 mutant complexes, our analysis reveals that high-affinity Spike mutations (including N440K, S443A, G476S, E484R, G502P) tend to cluster near known human ACE2 recognition sites (K31 and K353).
Introduction: We found that 31 high-affinity S mutations, including N440K, S443A, G476S, E484R, G502P, are clustered in the vicinities of two known interaction hotspots of hACE2.
Result: Among the antibody escape mutants identified using a cell-based


  Mutations in the SARS-CoV-2 spike protein modulate the virus affinity to the human ACE2 receptor, an in silico analysis.
 PMID: 33883984       2021       EXCLI journal
Result: The substitutions G476A, K444N, N440K, Q493K, Q493L, and Q493R were identified as stabilizing by the DUET software.


  Structure-Function Analyses of New SARS-CoV-2 Variants B.1.1.7, B.1.351 and B.1.1.28.1: Clinical, Diagnostic, Therapeutic and Public Health Implications.
 PMID: 33803400       2021       Viruses
Result: Finally, in terms of binding energy, the highest affinity of C135 was found with N440K (-45.03 +- 12.14 kcal/mol) followed by N501Y (-28.63 +- 16.20 kcal/mol) and wildtype (-25.86 +- 13.10 kcal/mol).
Result: Finally, in the case of N440K, the total number of hydrogen bond interactive residues was found to be 12.
Result: However, in India, the N440K high frequency variant was observed to be located at the C135-RBD interaction interface, where the mutation led to a weaker interaction network (Figure S3C,D).


  Partial resistance of SARS-CoV-2 Delta variants to vaccine-elicited antibodies and convalescent sera.
 PMID: 34723159       2021       iScience
Abstract: Highly transmissible SARS-CoV-2 variants identified in India and designated B.1.617, Kappa (B.1.617.1), Delta (B.1.617.2), B.1.618, and B.1.36.29 contain spike mutations L452R, T478K, E484K, E484Q, and N440K located within the spike receptor-binding domain and thus could contribute to increased transmissibility and potentially allow re-infection or cause resistance to vaccine-elicited antibody.


  SARS-CoV-2 Variants, RBD Mutations, Binding Affinity, and Antibody Escape.
 PMID: 34829998       2021       International journal of molecular sciences
Introduction: There have been a number of missense mutations observed in the receptor-binding domain (RBD) of the SARS-CoV-2 S protein, which have presented in one or more of the VOCs, including the N440K, G446V, L452R, Y453F, E484Q, F490S, N501Y, N501S, E484K, and K417N, most of which are located at the RBD-ACE2 interface.


  Elucidating the role of N440K mutation in SARS-CoV-2 spike - ACE-2 binding affinity and COVID-19 severity by virtual screening, molecular docking and dynamics approach.
 PMID: 34904526       2021       Journal of biomolecular structure & dynamics
Abstract: The N440K strain escapes from antibody neutralization, which might increase reinfection and decrease vaccine efficiency.
Abstract: The frequency of N440K variant was higher during the second wave in South India.
Abstract: To find a potential inhibitor against mutant N440K SARS-CoV-2, a virtual screening process was carried out and found ZINC169293961, ZINC409421825 and ZINC22060839 as the best binding energy compounds.


  Molecular Characterization of Severe Acute Respiratory Syndrome Coronavirus 2 Isolates From Central Inner Sardinia.
 PMID: 35095827       2021       Frontiers in microbiology
Table: p.Asn440Lys
Discussion: Some globally rare (~1% or less) spike substitutions in the RBD were identified, namely R346S, K417N, and N440K.



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