A bioluminescent and homogeneous SARS-CoV-2 spike RBD and hACE2 interaction assay for antiviral screening and monitoring patient neutralizing antibody levels.
Abstract: In contrast, while E484K mutation did not highly change the binding affinity, it still escaped antibody inhibition likely due to changes in the epitope recognized by the antibody.
Result: Antibody 5 displayed reduced binding to RBD-Fc E484K, while antibody 14 showed intermediate binding toward all RBD-Fc tested.
Result: The E484K mutation impaired inhibition by antibody 5.
Result: The E484K mutation that is common in many of the virus variants showed a twofold decrease in affinity to hACE2.
Result: These results prompted us to investigate the effect of mutations E484K, Y453F and N501Y on the binding of neutralizing antibodies described in.
The D614G Virus Mutation Enhances Anosmia in COVID-19 Patients: Evidence from a Systematic Review and Meta-analysis of Studies from South Asia.
Discussion: For example, the virus with the N501Y mutation has similar binding to ACE2, while the K417N and the E484K mutants may have slightly increased binding to ACE2.
In vitro selection of Remdesivir resistance suggests evolutionary predictability of SARS-CoV-2.
Method: The receptor binding domain of Spike is from amino acids 319-541: B1.351 and P1 had 3 mutations in the RBD (K417N/T, E484K and N501Y) while Alpha (B.1.1.7) only had one (N501Y).
Method: We used the following amino acids replacements and deletions in Spike for each lineage-based COG-UK defined changes for each lineage; Beta (B1.351; L18F, D80A, D215G, R246L, K417N, E484K, N501Y, A701V), Gamma (P.1;
Contribution of single mutations to selected SARS-CoV-2 emerging variants spike antigenicity.
Introduction: Similarly, the E484K and K417N/T mutations in the RBD that were first described in the B.1.351 and P.1 lineages likely due to immune evasion from vaccine or natural infection-elicited antibodies, are now present in several other lineages.
Result: No major changes were observed for the E484K mutation.
Result: Of note, the E484K mutation, also found in the RBD of other emerging variants (P.1 and B.1.526) did not significantly impact the ACE2-Fc interaction.
Figure: N, (D) K417T, (E) E484K, and (F)
Figure: N, (D) K417T, (E) E484K, and (F).
The emergence and ongoing convergent evolution of the SARS-CoV-2 N501Y lineages.
Introduction: Although both the K417N and K417T mutations can reduce the affinity of Spike for ACE2, in conjunction with the N501Y and E484K mutations, ACE2 binding is restored to that of wild-type Spike.
Introduction: Crucially, E484K and other mutations at S/484 also frequently confer protection from neutralization by both convalescent sera, vaccine-elicited antibodies, and some monoclonal antibodies.
Introduction: The vast majority of V2 and V3 variants and ~0.3% of more recent samples of V1 variants also have a Spike E484K mutation.
Introduction: There is therefore increasing evidence that viruses carrying the
Whole Genome Sequencing of SARS-CoV-2 Strains in COVID-19 Patients From Djibouti Shows Novel Mutations and Clades Replacing Over Time.
Receptor binding, immune escape, and protein stability direct the natural selection of SARS-CoV-2 variants.
PMID: 34543625
2021
The Journal of biological chemistry
Abstract: Compared with the wildtype, four mutants (K417N, Y453F, N501Y, and K417T/E484K/N501Y) had weaker affinity for the CC12.1 antibody, whereas two (S477N and S494P) had similar affinity, and two (T478I and E484K) had stronger affinity than the wildtype.
Abstract: Of the eight best-expressed mutants, two (N501Y and K417T/E484K/N501Y) showed stronger affinity to angiotensin-converting enzyme 2 compared with the wildtype, whereas four (
Table: E484K
Case Report: Paucisymptomatic College-Age Population as a Reservoir for Potentially Neutralization-Resistant Severe Acute Respiratory Syndrome Coronavirus 2 Variants.
PMID: 34544043
2021
The American journal of tropical medicine and hygiene
Conclusion: It was recently reported that there are four major epitope classes on the SARS-CoV-2 spike protein receptor-binding domain where neutralizing antibodies bind, and that Q493R (BV-1) and E484K (not found in BV-1, but important in B.1.351 and B.1.617 variants) mediate roughly equivalent levels of resistance to only class-2 neutralizing antibodies, as defined in that study.
Review of the mechanisms of SARS-CoV-2 evolution and transmission.
Conclusion: We forecast that a few co-mutation sets, including [A411S, L452R, T478K], [L452R, T478K, N501Y], [K417N, L452R, T478K], [L452R, T478K, E484K, N501Y], and [P384L, K417N, E484K, N501Y], have a great potential to grow into unprecedentedly dangerous new SARS-CoV-2 variants.
Introduction: A list of vaccine-escape (vaccine-breakthrough) mutations was tabulated in our early work, including
Rapid Identification of Neutralizing Antibodies against SARS-CoV-2 Variants by mRNA Display.
Abstract: A potent ACE2-blocking nAb was further engineered to sustain binding to S RBD with the E484K and L452R substitutions found in multiple SARS-CoV-2 variants.
SARS_CoV_2 mutation literature information.
PMID: 
2021
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