literature

SARS_CoV_2 mutation literature information.

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,).

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

SARS-CoV-2 receptor-binding mutations and antibody contact sites.

PMID: 34386694 2021 Antibody therapeutics

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.

Mutational analysis in international isolates and drug repurposing against SARS-CoV-2 spike protein: molecular docking and simulation approach.

PMID: 34307771 2021 Virusdisease

Table: A475V

Ongoing global and regional adaptive evolution of SARS-CoV-2.

PMID: 34292871 2021 Proc Natl Acad Sci U S A

Result: N234Q, A475V, and V483A were never or rarely found in our alignment, but L452R is a signature of variant B.1.429.

Result: Four more substitutions in the RBD, among others, N234Q, L452R, A475V, and V483A, have been demonstrated to confer antibody resistance.

Insilico study on the effect of SARS-CoV-2 RBD hotspot mutants' interaction with ACE2 to understand the binding affinity and stability.

PMID: 34217923 2021 Virology

Result: All other 11 mutations (N501I, N501S, N501T, N501Y, Q493L, Q493H, A475V, L455F, G446S and K417R) were predicted to have a neutral effect on the protein function.

Result: However, T when replaced with S at position 500 reduces the binding affinity between RBD and ACE2, whereas the variants L455F and A475V increase their binding affinity.

Result: The point mutations L455F, A475V and T500

Epitope Classification and RBD Binding Properties of Neutralizing Antibodies Against SARS-CoV-2 Variants of Concern.

PMID: 34149735 2021 Frontiers in immunology

Result: A second group of RBD variants, L452R (15%), G446V (10%), and N440Y (5%) disrupted fewer NAb interactions, while all NAbs bound efficiently (>50%, relative to WT reference) to RBD variants T345I, A475V, and Y505W.

Result: Based on the in silico NAb epitope analysis, nine RBD variants that localize to the C1 (K417T, A475V, N501Y, Y505W), C1D/C2 (G446V, L452R and E484K) and C3 epitopes (T345I<

Vaccine-escape and fast-growing mutations in the United Kingdom, the United States, Singapore, Spain, India, and other COVID-19-devastated countries.

PMID: 34004284 2021 Genomics

Table: A475V

SARS-CoV-2 mutations: the biological trackway towards viral fitness.

PMID: 33928885 2021 Epidemiology and infection

Introduction: Several mutations including A475V, N439K, L452R, F490L, V483A and Y508H in S protein resulted in decreased sensitivity to mAb.

Table: A475V

Mutations in the SARS-CoV-2 spike protein modulate the virus affinity to the human ACE2 receptor, an in silico analysis.

PMID: 33883984 2021 EXCLI journal

Abstract: By applying molecular docking using both Z-Dock and Haddock software we found that multiple mutations, including A475V, V455E, V445L, and V445I, resulted in the higher binding free energy as compared to the wild type (WT) spike protein, thus had a destabilizing effect on the binding to ACE2.

Result: Several mutants, including A475V, V455E, V445L, and V445I interacted with the higher binding free energy of -10.7 kcal/mol, -11.2 kcal/mol, -11.4 kcal/mol, and -10.8 kcal/mol, respectively, resulting in less stable interaction with ACE2 than the WT spike protein.

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