SARS-CoV-2 mutations acquired during serial passage in human cell lines are consistent with several of those found in recent natural SARS-CoV-2 variants.
PMID: 35474907
2022
Computational and structural biotechnology journal
Result: In addition, E484D mutations were observed in all viruses, including the original strain.
Discussion: Although this site was ultimately selected as aspartate (D) after 12 passages in all cell types, it may be crucial for viral adaptation in host cells; importantly, E484K and E484D have been associated with a protective immune response and viral permissiveness in several host cells.
Discussion: An E484D substitution on the spike protein was found in all viruses, including the original isolate used here, compared to the SARS-CoV-2 reference genome (Wuhan-Hu-1, GenBank Accession no.
Discussion: The E484D mutation may have been generated in the passaging process, allowing replication in the A549 cells in this study.
Influence of treatment with neutralizing monoclonal antibodies on the SARS-CoV-2 nasopharyngeal load and quasispecies.
PMID: 34537363
2022
Clinical microbiology and infection
Introduction: The full spectrum of key spike mutations associated with resistance to mAbs is not yet established, but mutations K417N, E484D/K/Q, Q493R/K and S494P seem to be involved in virus escape and resistance to mAbs.
Introduction: In an escape mutation study, which using 19 monoclonal antibodies, substitutions were found at E484 with higher incidence than at any other residue, and four variants at this position (E484A, E484D, E484G, and E484K) exhibited resistance to each of the human convalescent sera tested.
Table: E484D
Allosteric Determinants of the SARS-CoV-2 Spike Protein Binding with Nanobodies: Examining Mechanisms of Mutational Escape and Sensitivity of the Omicron Variant.
PMID: 35216287
2022
International journal of molecular sciences
Result: Moreover, mutations at the E484 position (E484A, E484G, E484D, and E484K) confer partial resistance to the convalescent plasma, showing that E484 is also one of the dominant epitopes of spike protein.
SARS-CoV-2 Omicron variant: Immune escape and vaccine development.
Abstract: Notably, mutation E484D largely rescued Huh-7 but not Vero cell entry from blockade by the neutralizing antibody Imdevimab and rendered Huh-7 cell entry ACE2-independent.
Abstract: These results suggest that the naturally occurring mutation E484D allows SARS-CoV-2 to employ an ACE2-independent mechanism for entry that is largely insensitive against Imdevimab, an antibody employed for COVID-19 therapy.
Abstract: We report that mutation E484D markedly increased SARS-CoV-2 S-driven entry into the hepatoma cell line Huh-7 and the lung cell NCI-H1299 without augmenting ACE2 binding.
Molecular rationale for SARS-CoV-2 spike circulating mutations able to escape bamlanivimab and etesevimab monoclonal antibodies.
Result: Interesting, replacing the viral spike E484 with each of the alternative residues consid
Discussion: 2A,B, Table S2), we considered all possible mutations actually reported at this position in circulating viral variants (i.e., E484A/D/G/K/Q/R/V), and found that all these amino acid variations should confer strong escaping ability to bamlanivimab.
Discussion: Spike variants identified in these studies that presented reduced susceptibility to the LY-CoV555 mAb included the following substitutions: E484D/K/Q, F490S, Q493R, and S494P.
Discussion: Moreover, the E484Q/V/A/G/D mutations have been just described by Chen et al.
A Combination of Receptor-Binding Domain and N-Terminal Domain Neutralizing Antibodies Limits the Generation of SARS-CoV-2 Spike Neutralization-Escape Mutants.
Discussion: Thus, the analysis of the SARS-CoV-2 spike gene shows the mutation of D614G that increases SARS-CoV-2 infectivity, whereas the E484D mutation was correlated with human immune serum neutralization resistance.
SARS_CoV_2 mutation literature information.
PMID: 
2022
Computational and structural biotechnology journal
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