SARS_CoV_2 mutation literature information.


  Targeted Sanger sequencing to recover key mutations in SARS-CoV-2 variant genome assemblies produced by next-generation sequencing.
 PMID: 35294336       2022       Microbial genomics
Abstract: We applied the primer set and wet-laboratory protocol to sequence 222 samples that were missing positions with key mutations K417N, E484K, and N501Y due to poor coverage after NGS sequencing.
Abstract: We successfully sequenced 153 samples of 222 (69 %) using Sanger sequencing and confirmed the occurrence of key beta variant mutations (K417N, E484K, N501Y) in the S genes of 142 of 153 (93 %) samples.


  The SARS-CoV-2 Delta variant induces an antibody response largely focused on class 1 and 2 antibody epitopes.
 PMID: 35313588       2022       bioRxiv
5Result: Notably, sublineages of the Delta variant, AY.1 and AY.2, colloquially referred to as ""Delta+"" lineages, contain the K417N mutation."
Result: K417N has a larger effect on neutralization in the Delta than in the D614G spike.
Result: Delta + E484K has an ~8-fold effect on neutralization for primary Delta-infection elicited antibodies, but only a ~3-fold effect for mRNA vaccination- or Delta breakthrough infection-elicited antibodies, comparable to the effect of Delta + K417N mutation.


  SARS-CoV-2 Omicron variant: Immune escape and vaccine development.
 PMID: 35317190       2022       MedComm
Abstract: Some noticeable mutations, including K417N, T478K, N501Y, and P681H, are shared with the previous VOCs Alpha, Beta, Gamma, or Delta variants and have been proven to be associated with higher transmissibility, viral infectivity, and immune evasion potential.
Introduction: Although the Omicron-specific RBD substitutions (K417N and E484A) reduced binding of the spike protein to ACE2, other mutations that increased the affinity for ACE2 could compensate for such effects.
Introduction: For instance, the K417N and N501Y mutations were known to confer protection against a number of mAbs.


  Omicron Variant of SARS-CoV-2 Virus: In Silico Evaluation of the Possible Impact on People Affected by Diabetes Mellitus.
 PMID: 35321335       2022       Frontiers in endocrinology
Abstract: In the Omicron variant, Lys417 mutates into an asparagine, preventing the possible non-enzymatic glycation of this residue.
Discussion: In the Omicron variant, Lys417 mutates into an asparagine, preventing the possible non-enzymatic glycation of this residue.


  Neutralisation Hierarchy of SARS-CoV-2 Variants of Concern Using Standardised, Quantitative Neutralisation Assays Reveals a Correlation With Disease Severity; Towards Deciphering Protective Antibody Thresholds.
 PMID: 35330908       2022       Frontiers in immunology
Result:
Result: Compared to the neutralisation titres against PVs bearing the ancestral Spike, we observed the following geometric mean fold changes in neutralisation titres: B.1.1.298: 1.1 fold decrease, B.1.1.7: 1.8 fold decrease, B.1.617.2 K417N: 3.1 fold decrease, B.1.617.2: 4.8 fold decrease, B.1.617.1: 4.9 fold decrease, P.1: 8.2 fold decrease and lastly, B.1.351: 8.3 fold decrease.
Discussion: In addition, the K417N mutation appears to increase the neutralisation efficiency compared to the original B.1.617.2.


  Early Genomic, Epidemiological, and Clinical Description of the SARS-CoV-2 Omicron Variant in Mexico City.
 PMID: 35336952       2022       Viruses
Result: K417N/T is present in the Alpha and Gamma variants, and both mutations facilitate immune escape for monoclonal antibodies (bamlanivimab/LY-CoV555), escape from neutralization by convalescent plasma, and escape by sera from BNT162b2-vaccinated individuals.
Result: Figure 3 shows the most frequent amino acid substitutions in the RBD (G339D, R346K, K417N, S371L, S373P, S375F, N440K, Q498R, and N501Y).
Result: We found that the substitutions R346K, K417N, and N440K were more preval


  Protective Immunity of the Primary SARS-CoV-2 Infection Reduces Disease Severity Post Re-Infection with Delta Variants in Syrian Hamsters.
 PMID: 35337002       2022       Viruses
Discussion: Comparable cell entry efficiency was reported by a recent study for the Delta sub-lineages with K417N mutation in comparison with the wildtype SARS-CoV-2 with the D614G mutation.
Discussion: Here, we observed a comparable neutralization efficiency in Delta AY.1-infected hamster sera against the Delta, B.1 and Beta variants, suggesting that the presence of the K417N mutation may not confer an advantage in terms of immune evasion, at least against these variants.
Discussion: Similar results of comparable neutralization efficiency of the Delta variant with the K417N mutation and the Delta variant has been reported in pseudo-virus neutralization studies.


  E-Volve: understanding the impact of mutations in SARS-CoV-2 variants spike protein on antibodies and ACE2 affinity through patterns of chemical interactions at protein interfaces.
 PMID: 35341044       2022       PeerJ
Introduction: One of those effects revealed by Nelson and collaborators is the increased affinity between the Receptor-Binding Domain (RBD) and the Angiotensin-Converting Enzyme 2 (ACE2) protein caused by the N501Y and E484K mutations, which also have their potentiality enhanced when possessing the K417N/T modification.
Introduction: The Beta variant has non-synonymous spike mutations such as LAL 242-244 deletion, D80A, D215G, E484K, N501Y, A701V, L18F, R246I, K417N, and D614G.
Discussion:


  The dynamics of circulating SARS-CoV-2 lineages in Bogor and surrounding areas reflect variant shifting during the first and second waves of COVID-19 in Indonesia.
 PMID: 35341058       2022       PeerJ
Discussion: For Delta variants, we observed 12 key amino acid changes in spike protein that were mostly similar to other studies, including S_T19R, S_T95I, S_G142D, S_E156-, S_F157-, S_R158G, S_K417N, S_L452R, S_T478K, S_D614G, S_P681R, and S_D950N .


  SARS-CoV-2-specific antibody and T-cell responses 1 year after infection in people recovered from COVID-19: a longitudinal cohort study.
 PMID: 35345417       2022       The Lancet. Microbe
Discussion: The three mutations characterising the beta variant (K417N, E484K, and N501Y) are located at the receptor-binding domain, making the variant resistant to some potent neutralising antibodies.



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