Investigation of nonsynonymous mutations in the spike protein of SARS-CoV-2 and its interaction with the ACE2 receptor by molecular docking and MM/GBSA approach.
PMID: 34346317
2021
Computers in biology and medicine
Introduction: found six distinct types of mutations namely, V367F, P384L, S438F, K439N, G476S, and V483A in RBD domain of the S-protein.
Table: V483A
Ongoing global and regional adaptive evolution of SARS-CoV-2.
Abstract: We unveil, for the first time, that high-frequency mutations R346K/S, N439K, G446V, L455F, V483F/A, F486L, F490L/S, Q493L, and S494P might compromise some of mAbs in clinical trials.
Anti-SARS-CoV-2 Vaccines and Monoclonal Antibodies Facing Viral Variants.
Introduction: It is characterized by nine mutations, and one deletion in the Spike, in particular H655Y, the 144 deletion (in common with 20I/501Y.V1), D215G (in common with 20H/501Y.V2), and V483A, near to the E484K residue in 20J/501Y.V3.
Introduction: It is characterized by nine mutations, and one deletion in the Spike; in particular, these include H655Y, which is also present in the 20J/501Y.V3 and 19B/501Y variants; the Y144 deletion common with 20I/501Y.V1; the D215G mutation in common with the 20H/501Y.V2 variant; and the V483A close to the E484 residue mutated in the 20J/501Y.V3 variant (E484K), which may be involved in post-vaccine or
V483A: an emerging mutation hotspot of SARS-CoV-2.
Abstract: V483A mutant virus is popular in North America with 36 cases so far and frequently occurring in recent days.
Abstract: One of the many mutations that have occurred in the viral genome is the V483A mutation, which is a part of the receptor-binding motif present in the S1 domain of the spike protein.
Abstract: This review compares the wild-type and the V483A mutants to analyze certain factors like the interaction between the virus and host-cell interface, binding affinity, stability, partition energy, hydrophobicity, occurrence rate and transmissibility.
Introduction: Apart from the primary (amino acid change) and secondary (loop structure) changes observed at the RBM of S protein due to V483A mutation, there are few gains in functions like higher solvent acce
V367F Mutation in SARS-CoV-2 Spike RBD Emerging during the Early Transmission Phase Enhances Viral Infectivity through Increased Human ACE2 Receptor Binding Affinity.
Result: V483A and V367F accounted for 11.59% and 11.26% of 302 mutants, respectively.
Result: All the mutants were clustered into 96 mutant types, six of which were dominant mutant types that were found in more than ten isolates (Table 1): V483A (35x), V367F (34x), V341I (23x), N439K (16x), A344S (15x), and G476S (12x).
Discussion: Among them, V483A in MERS-CoV and N439K in SARS-CoV resulted in reduced host receptor binding.
Characterization of SARS-CoV-2 different variants and related morbidity and mortality: a systematic review.
PMID: 34103090
2021
European journal of medical research
Table: V483A
Machine Learning Reveals the Critical Interactions for SARS-CoV-2 Spike Protein Binding to ACE2.
PMID: 34086459
2021
The journal of physical chemistry letters
Introduction: As expected, several mutations that were observed initially yet never became widespread, namely, G476S, V483A, and V367F, had negligible or slightly detrimental effects on binding to ACE2 (Table 2).
Introduction: Such is the case, for example, for G476S, V483A, and V367F.
Table: V483A
A core-shell structured COVID-19 mRNA vaccine with favorable biodistribution pattern and promising immunity.
PMID: 34059617
2021
Signal transduction and targeted therapy
Discussion: Although some of the mutations occurred in RBD region such as V367F, G476S, V483A, SW0123-elicited Abs were still able to neutralize these variants effectively, which suggested that diversified NAbs and non-RBD region functional Abs can be induced.
Vaccine-escape and fast-growing mutations in the United Kingdom, the United States, Singapore, Spain, India, and other COVID-19-devastated countries.
Result: We can see that VE mutations F490S, L452R, VW mutations F490L, N501Y, V483A, and N501T have relatively high BFE changes of the binding of S protein and ACE2, suggesting that they are high-risk mutations.