Introduction: The P.1 lineage-defining mutations in the Spike protein, especially in the receptor-binding domains (RBD) such as K417T, E484K and N501Y, are of concern because they may enhance ACE2 affinity and contribute to antibody evasion.
Table: E484K
Discussion: According to our results, most of the P.1 sequences carried the 22 lineage-defining mutations, including the three mutations in the Spike protein, RBD domain (K417T, E484K and N501Y) associated with evasion of the immune system and greater transmissibility.
mRNA vaccine-induced antibodies more effective than natural immunity in neutralizing SARS-CoV-2 and its high affinity variants.
Introduction: N501Y and two other mutations in the RBD domain, K417N/T and E484K, were subsequently founds in SARS-CoV-2 variants from South Africa (B.1.351) and Brazil (P.1).
Discussion: Other RBD mutations, K417N/T and E484K, either alone or in combinations, have not been evaluated in this study.
Characterization of the immune resistance of SARS-CoV-2 Mu variant and the robust immunity induced by Mu infection.
PMID: 35176774
2022
The Journal of infectious diseases
Abstract: Here we reveal that the two mutations in the SARS-CoV-2 Mu spike protein, YY144-145TSN and E484K, are responsible for the resistance to COVID-19 convalescent sera during early 2020 and vaccine sera.
SARS-CoV-2 infections in mRNA vaccinated individuals are biased for viruses encoding spike E484K and associated with reduced infectious virus loads that correlate with respiratory antiviral IgG levels.
Abstract: Fourteen of the amino acid substitutions, including N501Y and E484K, and nine deletions are located in the spike protein.
Introduction: In the receptor binding domain (RBD), in addition to the well-known substitutions N501Y and E484K, several changes were predicted to significantly affect the neutralizing epitopes.
Introduction: Subsequent detection of three mutations in the spike gene in a qPCR assay to screen for variants, as performed routinely in France in cases of SARS-CoV-2 positivity, revealed an atypical combination with L452R negativity, E484K positivity, an
Table: E484K
SARS-CoV-2 infections in mRNA vaccinated individuals are biased for viruses encoding spike E484K and associated with reduced infectious virus loads that correlate with respiratory antiviral IgG levels.
Introduction: E484 is an immunodominant spike protein residue and the E484K substitution enables the escape from neutralizing antibody inhibition in vitro and it may be linked with reduced vaccination efficacy.
Introduction: In February 2021 Public Health England (PHE) published a report of Alpha (formerly B.1.1.7) genomes with acquisition of the E484K spike mutation.
Introduction: Notably, the presence of the E484K mutation into the Alpha background led to a more-substantial loss of neutralizing activity by vaccine-elicited antibodies compared with the mutations in Alpha alone, suggesting that this variant represents a threat to the efficacy of the BNT162b2 mRNA vaccine.
Introduction: The Beta (formerly B.1.351) and Gamma (formerly P.1) variants were of particular concern because they carry the mu
SARS-CoV-2 infections in mRNA vaccinated individuals are biased for viruses encoding spike E484K and associated with reduced infectious virus loads that correlate with respiratory antiviral IgG levels.
Conclusion: In conclusion, sufficient neutralizing antibodies in Japanese participants after BNT162b2 vaccination were produced against the original, R.1 lineage, and Alpha variants of SARS-CoV-2, while an insufficient humoral immunity was observed against the Beta and Delta variants, indicating that the E484K mutation is not the sole factor contributing toward a weakened humoral response.
Discussion: Additionally, our data demonstrated that a lower antibody response was observed against the Beta variant, and not against the R.1 lineage variant, which indicates that the weak antibody response against the Beta variant was not solely due to the E484K mutation.
Discussion: Previous reports demonstrated that although the E484K mutation of Beta variants might cause humoral immunity escape, the combination of N501Y and K41
In silico investigations of heparin binding to SARS-CoV-2 variants with a focus at the RBD/ACE2 interface.
PMID: 35194375
2022
Process biochemistry (Barking, London, England)
Abstract: Herein, using the molecular docking and interaction energy analysis, we showed that N501Y, L452R-E484Q, and E484K mutations bind strongly with heparin in the range of - 7.4 to - 8.0 kcal/mol.
Abstract: The triple mutations, K417N-E484K-N501Y, and K417T-E484K-N501Y displayed weaker binding affinity to heparin (-6.6 kcal/mol).
Table: E484K
Figure: Two-dimensional (2D) diagrams of heparin-RBD interactions for (A) E484K, (B) N501Y, (C) L452R
Misidentification of the SARS-CoV-2 Mu variant using commercial mutation screening assays.
Introduction: Following the scheme described above, in August 2021, we detected three strains that presented K417N, N501Y, and E484K mutations but did not present delH69/V70, W152C, K417T, L452R, or V1176F mutations.
Introduction: Samples containing E484K and N501Y mutations and lacking delH69/V70 mutation were also subjected to rRT-PCR melting curve analysis of K417N and V1176F (VirSNiP Assays, TIB MOLBIOL, Germany), as this assay was commercially available before the Allplex SARS-CoV-2 Variants II Assay.
Introduction: The first assay, Allplex SARS-CoV-2 Variants I Assay (Seegene, Korea), inclu
Spread of Gamma (P.1) Sub-Lineages Carrying Spike Mutations Close to the Furin Cleavage Site and Deletions in the N-Terminal Domain Drives Ongoing Transmission of SARS-CoV-2 in Amazonas, Brazil.
Discussion: One of the most divergent Gamma sequences detected in Brazil was a P.1.4 lineage variant sampled in the Amazonas in October 2021 (EPI_ISL_5621224) that harbors 20 S mutations (eight more than the parental P.1 lineage), including several in common with (Delta144, Q498R, N501Y, H655Y, and N679K) or like (T95N, K417T, and E484K) those detected in Omicron.
Emergency SARS-CoV-2 Variants of Concern: Novel Multiplex Real-Time RT-PCR Assay for Rapid Detection and Surveillance.
SARS_CoV_2 mutation literature information.
PMID: 
2022
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