Abstract: Hence, we developed a PCR-based method to rapidly detect the 6 mutational hotspots (H49Y, G476S, V483A, H519Q, A520S, and
Discussion: Among frequent mutations observed in the S protein, a non-synonymous mutation, V483A, which increases the binding with ACE2 receptor, was mainly identified in the viral genomes isolated from North Americans.
Discussion: Moreover, the D614G showed the highest host entry activity among mutations such as V367F, G476S, V483A, and H49Y that frequently occur in the S protein.
Mutational analysis of structural proteins of SARS-CoV-2.
Method: Alternatively, lentivirus Lenti-GF1-SARS-CoV-2Delta19AA truncated spike envelope displaying the H49Y, S247R, V367F, R408I, V483A, H519Q, A520S, and D614G mutations was produced using the same method.
Result: To determine if natural infection induced broadly neutralizing Abs, we tested neutralization of pseudotyped viruses with spike protein variants in the S1 N-terminal domain (H49Y, V247R, V367F, R408I), in the receptor-binding domain ( PMID: 33758785
2021
Heliyon
Table: V483A
Structural stability predictions and molecular dynamics simulations of RBD and HR1 mutations associated with SARS-CoV-2 spike glycoprotein.
PMID: 33618621
2021
Journal of biomolecular structure & dynamics
Abstract: We have studied the impact of mutations such as A348T, N354D, D364Y, G476S, V483A, S494D in the RBD (319-591), and S939F, S940T, T941A, S943P (912-984) in the HR1 domains of spike glycoprotein.
Potentially adaptive SARS-CoV-2 mutations discovered with novel spatiotemporal and explainable AI models.
Result: Likewise, the spike protein harbored three non-synonymous mutations, including V483A in the receptor-binding domain (RBD).
Discussion: Among all the frequent mutations in this protein, the V483A mutation has been identified in this receptor and found mainly in SARS-CoV-2 genomes isolated from USA.
Variations in SARS-CoV-2 Spike Protein Cell Epitopes and Glycosylation Profiles During Global Transmission Course of COVID-19.
Result: Among them, amino acid substitutions T29I, G476S, D936Y, S943P, and P1263L changed the length of the linear B cell epitopes, whereas V483A, Q675H, and A706V had no influence on the length of linear epitopes, and the others had no effect on linear B cell epitopes (Table 1).
Result: Binding level results of T29I, V367F, A706V, and A831V demonstrated that these substitutions had low binding affinity in HLA-A01:01, HLA-B07:02, and HLA-B35:01 compared to the wild type, while H49Y, Q239K, PMID: 32577641
2020
bioRxiv
Result: First, we investigated Sarbecovirus conservation of 14 amino acids in the spike protein in which mutations appear to be accumulating in the SARS-CoV-2 population, namely D614G, L5F, L8V/W, H49Y, Y145H, Q239K, V367F, G476S, V483A, V615I/F, A831V, D839Y/N/E, S943P, P1263L.
Result: In contrast, L5F, L8V/W, H49Y, PMID: 32884216
2020
Journal of laboratory physicians
Abstract: Other mutations observed within RBD exhibiting low antigenicity were T323I, A344S, R408I, G476S, V483A, H519Q, A520S, A522S and K529E.
Result: Other speculated mutations in the putative epitopes lying within RBD showing less antigenicity were T323I, A344S, R408I, G476S, V483A, H519Q, A520S, A522S, and
ViMRT
SARS_CoV_2 mutation literature information.
PMID: 
2021
Gene reports
