Result: A number of these variants have RBD mutations such as L452R, E484K, and/or N501Y, which are thought to promote human ACE2 binding.
Result: B.1.1.7/E484K, Iota/B.1.526 + E484K (first associated with infections in New York), Eta/B.1.525 (a variant with associations with West Africa), and L452R (in multiple variants of concern, including Epsilon/B.1.427/B.1.429, first associated with infections in California, and Delta/B.1.617.2, which is currently replacing all other SARS-CoV-2 lineages globally) all allowed pseudovirus to use ferret ACE2 for cell
Figure: Alpha also known as B.1.1.7; Beta also known as B.1.351; Gamma also known as P.1; Eta also known as B.1.525; Iota also known as B.1.526 + E484K.
Comparative analyses of IgG/IgA neutralizing effects induced by three COVID-19 vaccines against variants of concern.
PMID: 35093484
2022
The Journal of allergy and clinical immunology
Abstract: Interestingly, all 3 vaccines could neutralize all tested variants of concern in addition to WT virus, but in some individuals, only low or no neutralization, especially against Alpha-E484K and the Delta variant, was detected.
Abstract: We also determined the neutralization ability against SARS-CoV-2 WT and B.1.1.7 (Alpha), B1.1.7 E484K (Alpha-E484K), B.1.351 (Beta), and B.1.617.2 (Delta) variants.
Pan-SARS neutralizing responses after third boost vaccination in non-human primate immunogenicity model.
Discussion: The Beta and Gamma variants are the most resistant to monoclonal antibodies (mAbs) and convalescent plasma from SARS CoV-2-infected individuals, and the resistance profiles correspond to several deletions in the N-terminal domain and the K417N/T, E484K/Q, and N501Y mutations in the RBD of SARS-CoV-2 Spike protein.
Discussion: The E484 position was identified as a dominant residue for escape from neutralizing activity by sera from COVID-19 convalescent patients with the E484K mutation in the SARS-CoV-2 Beta variant as the key factor responsible for the reduced neutralization potency of c
Mutations in the receptor-binding domain of human SARS CoV-2 spike protein increases its affinity to bind human ACE-2 receptor.
PMID: 35109768
2022
Journal of biomolecular structure & dynamics
Abstract: Here, we use the crystal structure of the RBD in complex with ACE-2 available in the public domain and analyse the 250 ns molecular dynamics (MD) simulations of wild-type and mutants; K417N, K417T, N440K, N501Y, L452R, T478K, E484K and S494P.
Divergent SARS-CoV-2 Omicron-reactive T and B cell responses in COVID-19 vaccine recipients.
Abstract: Further, we engineer a potent ACE2-blocking nAb to sustain binding to S RBD with the E484K and L452R substitutions found in multiple SARS-CoV-2 variants.
Result: E484K:an escape mutant found in many different variants, including B.1.351 and A.VOI.V2 :did, however, reduce the binding affinity of N-612-017 by 6- to 10-fold (Figures 6A and 6B).
Result: Generation of E484K- and L452R-resistant N-612-017.
Result: Interestingly, both N-612-017-01 and N-612-017-03 subclones not only exhibited restored binding affinity against E484K-expressing RBD variants, but they had 10- to 20-fold enhanced affinity against wild-type RB
Breadth of SARS-CoV-2 Neutralization and Protection Induced by a Nanoparticle Vaccine.
Introduction: Some of the substitutions in these variants have been detected arising independently on multiple genetic backgrounds, such as the spike substitutions N501Y, E484K or the 69-70 deletion, supporting a model of convergent evolution.
Result: Two other closely studied spike substitutions, E484K and L452R, were not notably enriched among vaccine breakthrough cases, and the D253G substitution was modestly depleted.
Introduction: The S protein E484Q mutation in the Kappa variant was similarly found in the Beta (B.1.351) and Gamma (P.1) lineages, where residue 484 is mutated to lysine (E484K).
Result: We have previously demonstrated the sensitivity of ab8 and S2M11 to the E484K mutation, wherein both antibodies were fully escaped.
Figure: The K484 surface potential was generated using the previously reported D614G + N501Y + E484K focus-refined atomic model.
Discussion: For example, the L452R mutation, mutations at position 484 (E484K and E484Q) and mutations within the N3 loop in the NTD (residues 141-156) have all been previously charact
SARS_CoV_2 mutation literature information.
PMID: 
2022
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