Method: The SARS-CoV-2 target sequences include (i) the wild-type (WT) gene fragment of S protein (S; nucleotides [nt] 21,563 to 25,384; GenBank accession number MN908947); (ii) the mutant gene fragments of S protein, including mutations L5F, D80A, D215G, R246I, K417N, L452R/Q, Y453F, T478K, E484Q/K, N501Y, A570D, D614G, P681H, A701V, T716I,
Evolutionary Tracking of SARS-CoV-2 Genetic Variants Highlights an Intricate Balance of Stabilizing and Destabilizing Mutations.
Crucial Mutations of Spike Protein on SARS-CoV-2 Evolved to Variant Strains Escaping Neutralization of Convalescent Plasmas and RBD-Specific Monoclonal Antibodies.
Figure: Eight mutations (Y453F, L455F, F456L, A475V, A475S, T500S, N501Y, and Y505H) were in the RBD and hACE2 interaction region (RBD/hACE2); 10 mutations (V367I, V382L, R408G, N438K, L452Q, S477N, T478K, E484Q, S494P, and A520S) were in the RBD region but no
The Emergence and Spread of Novel SARS-CoV-2 Variants.
5Result: Cluster 5 (also known as ""DeltaFVI-spike""): Some researchers found that mutation Y453F in the RBD of S protein of this variant did not reduce existing humoral immunity or affect the neutralization response, but it increased transmissibility due to its enhanced affinity with ACE2."
Result: In addition, Y453F is a high mutation frequency of 1,075, but its role is unclear.
Identification of natural compounds as SARS-CoV-2 entry inhibitors by molecular docking-based virtual screening with bio-layer interferometry.
8Discussion: These include N439K (B.1.141 ""Scottish lineage""), Y453F (B.1.1.298 ""mink variant""), N501Y (B.1.1.7, B.1.351 and P1) and D614G (found in most variants)."
Abstract: The EGCG was further validated with no observable animal toxicity and certain antiviral effect against SARS-CoV-2 pseudovirus mutants (D614G, N501Y, N439K & Y453F).
Introduction: The Y453F mutant was originated from mammal mink and has infectivity on humans.
Method: For pseudovirus assay, wild-type and 4 mutants (D614G, N501Y, N439K & Y453F)
SARS-CoV-2 receptor-binding mutations and antibody contact sites.
Discussion: Furthermore, there were a number of mutations that could significantly improve RBD-ACE2 binding but were either completely absent in our data or of extremely low frequency, including N501F, Y453F, T385R, Q493M, and Q414A, among others (Supplementary Table 3).
Signatures in SARS-CoV-2 spike protein conferring escape to neutralizing antibodies.
Introduction: Corroborating the potential biological relevance of those recurrent mutations, some of them are predicted to affect SARS-CoV-2 affinity to ACE-2 receptors (e.g., Y453F), to be potentially involved in immune evasion (e.g., E484K), or to increase entry efficiency (e.g., DeltaH69/DeltaV70).
Mutational analysis in international isolates and drug repurposing against SARS-CoV-2 spike protein: molecular docking and simulation approach.
Discussion: Following the findings of mutations in NTD, mutations were also found in CTD/RBD of the SARS-CoV-2 spike sequence including Y453F and V367F.
SARS_CoV_2 mutation literature information.
PMID: 
2021
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