Result: Second, among the top 25 most observed RBD mutations, T478K, L452Q, N440K, L452R, N501Y, N501T, F490S, A475V, and P384L are the 8 most infectious ones judged by their ability to strengthen the binding with ACE2, as shown in Figure 1c.
Table: A475V
E484K and N501Y SARS-CoV 2 spike mutants Increase ACE2 recognition but reduce affinity for neutralizing antibody.
PMID: 34915409
2022
International immunopharmacology
Table: A475V
A comprehensive overview of identified mutations in SARS CoV-2 spike glycoprotein among Iranian patients.
Introduction: While most of alterations in the receptor binding domain (RBD) reduce infectivity, A475V, L452R, V483A, and F490L variants induce resistance to some neutralizing antibodies.
Novel Monoclonal Antibodies and Recombined Antibodies Against Variant SARS-CoV-2.
Abstract: Compared with XG81, XG83 exhibited a higher RBD binding affinity and neutralization potency against wild-typed pseudovirus, variant pseudoviruses with mutated spike proteins, such as D614G, E484Q, and A475V, as well as the authentic SARS-CoV-2 virus.
Introduction: A475V variant at RBD has also been reported to become resistant to some nAbs.
Introduction: Moreover, the recombined antibodies (rAbs) with heavy and light chains from different nAbs produced some new antibodies with a higher neutralization p
Discussion: Both XG81 and XG83 could effectively neutralize against Wuhan, E484Q, A475V, and D614G pseudoviruses.
Ongoing global and regional adaptive evolution of SARS-CoV-2.
Introduction: Finally, it has been reported that the antibody neutralization sensitivity of some RBD mutants including A475V, F490L, and V483A (among others) is reduced, suggesting that SARS-CoV-2 is mutating to evade neutralization/RBD binding.
Characterization of SARS-CoV-2 worldwide transmission based on evolutionary dynamics and specific viral mutations in the spike protein.
PMID: 34419160
2021
Infectious diseases of poverty
Table: A475V
Myxobacterial depsipeptide chondramides interrupt SARS-CoV-2 entry by targeting its broad, cell tropic spike protein.
PMID: 34463219
2021
Journal of biomolecular structure & dynamics
Introduction: The top-binding ligands were additionally screened against biologically significant SARS-CoV-2 mutations occurring in the RBD of the S protein such as N501Y, E484K,
Method: Using the same PDB ID, the SARS-CoV-2 variants (N501Y, E484K, K417N/T, A475V, L452R, V483A, F490L, S477N, N439K) were constructed using UCSF chimera platform by editing necessary amino acids of the S protein via the swapaa command which utilizes information from a rotamer library (Shapovalov & Dunbrack,).
Comprehensive mapping of binding hot spots of SARS-CoV-2 RBD-specific neutralizing antibodies for tracking immune escape variants.
Result: We demonstrated that some mutations, namely, K417A, F456A, N460A, A475V, F486A, and N487A, led to less binding for multiple group 1 antibodies.