SARS_CoV_2 mutation literature information.


  The D614G Virus Mutation Enhances Anosmia in COVID-19 Patients: Evidence from a Systematic Review and Meta-analysis of Studies from South Asia.
 PMID: 34533304       2021       ACS chemical neuroscience
Discussion: For example, the Alpha variant that often also has N501Y, N439K, and Y453F mutations appears to require a deletion (DeltaH69/V70) in the spike protein to maintain optimal cleavage and infectivity.


  Receptor binding, immune escape, and protein stability direct the natural selection of SARS-CoV-2 variants.
 PMID: 34543625       2021       The Journal of biological chemistry
Introduction: These include 9 single site mutations K417N, N439K, Y453F, S477N, S477I, T478I, E484K, S494P and N501Y (Alpha variant), a double mutant (E484K/N501Y) and two triple mutants (K417N/E484K/N501Y (Beta variant) and
Result: Among 9 single site mutants, 2 mutants (N439K and S477I) did not express very well and appreciable amount of protein needed for binding studies could not be obtained for these mutants.


  Additional Positive Electric Residues in the Crucial Spike Glycoprotein S Regions of the New SARS-CoV-2 Variants.
 PMID: 34880635       2021       Infection and drug resistance
Table: N439K


  Prediction of the Effects of Variants and Differential Expression of Key Host Genes ACE2, TMPRSS2, and FURIN in SARS-CoV-2 Pathogenesis: An In Silico Approach.
 PMID: 34720581       2021       Bioinformatics and biology insights
Result: We also analyzed the effect of 27 missense variants of SARS-CoV-2 spike protein (RBD) on the binding interaction of spike protein with ACE2 and observed that L452Q, T478K, L455F, F456L, S459F, A475V, N439K, L452R, T470N, E484D, E484A, E484K, E484Q, F486L, S494P, S494L, N501T,  PMID: 34805715       2021       ACS omega
Result: For example, a recent study showed that N439K compensated for an RBM mutation K417V that otherwise decreases the receptor-binding affinity and that several mAbs were more sensitive to these mutations in combination versus individually.


  The alpha/B.1.1.7 SARS-CoV-2 variant exhibits significantly higher affinity for ACE-2 and requires lower inoculation doses to cause disease in K18-hACE2 mice.
 PMID: 34821555       2021       eLife
Result: Determination of the evasion capacity of the N439K and N501Y variants in naturally induced antibody-mediated immunity.
Result: However, best-fit IC50 values from sera from mice immunized with spike differed slightly between strains, as 11% and 19% higher serum concentration was required for the N439K and N501Y variants, respectively, to achieve the same inhibition levels as for the wt RBD.
Result: Linear regression and Spearman correlation analyses of the mAbs with best-fit IC50s within the range of concentration tested (n = 8) showed that the N439K and N501Y mutations had very minor effects on the inhibition potency of the mAbs (N439K R2 = 0.9777, rho = 1, p <


  A Conservative Replacement in the Transmembrane Domain of SARS-CoV-2 ORF7a as a Putative Risk Factor in COVID-19.
 PMID: 34943191       2021       Biology
Abstract: Well-characterized mutations in the spike protein, such as D614G, N439K, Delta69-70, E484K, or N501Y, are currently defining specific variants; however, some less studied mutations outside the spike region, such as p.


  Low Represented Mutation Clustering in SARS-CoV-2 B.1.1.7 Sublineage Group with Synonymous Mutations in the E Gene.
 PMID: 34943523       2021       Diagnostics (Basel, Switzerland)
Abstract: Interestingly, these samples also harbored three other mutations (S137L-Orf1ab; N439K-S gene; A156S-N gene), which had a very low diffusion rate worldwide.
Introduction: Thus, the samples were sequenced, which revealed the presence of a synonymous mutation (c.26415 C > T, TAC > TAT, Reference Genome: NC_045512) in the E gene and three other mutations (S137L:Orf1ab gene, N439K:Spike gene, and A156S:Nucleocapsid gene) scattered throughout the genome in all samples carrying the  PMID: 34700382       2021       mBio
Abstract: Through in silico protein structure prediction and immunoinformatics tools, we discovered D614G is the key determinant to S protein conformational change, while variations of N439K, T478I, E484K, and N501Y in S1-RBD also had an impact on S protein binding affinity to hACE2 and antigenicity.
Introduction: Besides D614G, amino acid changes within S1-RBD, such as N439K, L452R, E484K/Q, and N501Y, also favor virus resistance to monoclonal antibody neutralization.
Discussion: SARS-


  The Development of SARS-CoV-2 Variants: The Gene Makes the Disease.
 PMID: 34940505       2021       Journal of developmental biology
Introduction: N439K has also been shown to enhance the binding affinity for the ACE2 receptor.
Introduction: Its appearance is recurrent and often co-occurs with N439K, Y453F, and N501Y mutations, suggesting a selective advantage and possible epistasis between mutations, which should be further examined.
Introduction: Mutation Y453F, along with N439K, G446V, K444E, and S477N, among others, which are located at the interface between the S1 and ACE2, have been shown to partially interfere with antibody binding and neutralization.



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