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.
Abstract: Discussion: Molecular dynamics simulations followed by Poisson-Boltzmann calculations corroborate the higher complementarity to the receptor and lower to the antibodies for the K417T/E484K/N501Y (Gamma) mutant compared to the wild-type strain, as pointed by E-Volve, as well as an intensification of this effect by changes at the protein conformational equilibrium in solution.
Abstract: Results: The results found in this study depict the highly frequent interface changes made by the entire set of mutations, mainly conducted by N501Y and E484K.|mgd
Method: A Gamma lineage RBD (with mutations E484K, N501Y, and K417T) was modelled comparatively using SWISS-MODEL.
SARS-CoV-2-specific antibody and T-cell responses 1 year after infection in people recovered from COVID-19: a longitudinal cohort study.
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.
AstraZeneca COVID-19 vaccine induces robust broadly cross-reactive antibody responses in Malawian adults previously infected with SARS-CoV-2.
Introduction: The beta variant bears genetic changes in the functional domain of the SARS-CoV-2 spike (S) protein including substitutions in the receptor-binding domain (RBD) (E484K, N501Y and K417N), four substitutions and a deletion in N-terminal domain (NTD) (L18F, D80A, D215G, L242H and R246I) and substitutions in S2 (D614G and A701V) regions.
Evasion of vaccine-induced humoral immunity by emerging sub-variants of SARS-CoV-2.
Introduction: Beta+R346K and Mu+K417N share the same haplotype with R346K, K417N, E484K and N501Y mutations in the receptor-binding domain (RBD) in the spike protein, as shown in Figure 2.
Introduction: In June, another variant harboring E484K and R346K was found in Angola with low neutralization titer against mRNA1273 vaccinated serum.
Discussion: A.VOI.V2 harbors R346K, T478R and E484K in the RBD.
Discussion: reported that neutralization efficacy was reduced for the Mu variant har
Impact of B.1.617 and RBD SARS-CoV-2 variants on vaccine efficacy: An in-silico approach.
PMID: 35370005
2022
Indian journal of medical microbiology
Result: Out of seven variants, B.1.617 (B.1.617 <Q493N < E484K < K486L < L455Y < R408I < K417G) demonstrates lowest binding energy against antibody.
Result: To examine the dynamic behavior, MD simulation runs for 10 ns to contemplate the structural stability of RBD mutant variants (F486L, Q493N, B.1.617, R408I, L455Y, K417G and E484K) in comparison to wild type.
Result: We found that seven mutant variants (F486L, Q493N, B.1.617 ( PMID: 35371108
2022
Frontiers in immunology
Discussion: The immune escape of some variants against LY-CoV555 may be related to the E484K/A mutation.
Insights into SARS-CoV-2's Mutations for Evading Human Antibodies: Sacrifice and Survival.
PMID: 33834772
2022
Journal of medicinal chemistry
Method: To simulate the binding between the RBD of the South Africa variant and ACE2, we obtained the crystal structure (PDB entry 6M0J) for the RBD-ACE2 complex and introduced three mutations (N501Y, K417N, and E484K) when preparing the .psf and .pdb files for the complex.
Discussion: Before the E484K mutation, E484 forms a hydrogen bond with F490 (Figure S5), which attaches the loop (residues 477-486) to the remainder of the RBD.
Discussion: In the South Africa variant (501Y.V2), actually there are two more mutations, N501Y and E484K.
Discussion: Therefore, the gain from the improved RBD-ACE2 binding that resulted from
First importations of SARS-CoV-2 P.1 and P.2 variants from Brazil to Spain and early community transmission.
PMID: 34099945
2022
Enfermedades infecciosas y microbiologia clinica
Abstract: The exportation of the P.2 variant, carrying the E484K mutation, deserves attention.
Conclusion: The P.2 variant carrying the E484K concern mutation is also reported here, imported by two other travellers who remained asymptomatic.
Introduction: A recent alarm has raised in the UK due to the acquisition of the same E484K mutation in 28 cases infected with the B.1.1.7 variant.
Introduction: However, P.2 carries the E484K substitution, shared by the P.1 and B.1.351 variants, which maps in the RBD (receptor binding domain) of the spike protein.
Emergence of the E484K Mutation in Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) Lineage B.1.1.345 in Upstate New York.
Abstract: A severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) B.1.1.345 variant carrying the E484K mutation was detected in 4 patients with no apparent epidemiological association from a hospital network in upstate New York.
Impact of Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) Variant-Associated Receptor Binding Domain (RBD) Mutations on the Susceptibility to Serum Antibodies Elicited by Coronavirus Disease 2019 (COVID-19) Infection or Vaccination.
SARS_CoV_2 mutation literature information.
PMID: 
2022
PeerJ
Browser Board
Co-occurred Entities
Filtrator
ViMRT