Non-RBM Mutations Impaired SARS-CoV-2 Spike Protein Regulated to the ACE2 Receptor Based on Molecular Dynamic Simulation.
PMID: 34386518
2021
Frontiers in molecular biosciences
Result: A new 493GLN (E21)-34HIS (O) hydrogen bond was generated in both the N354D and V367F systems after excluding the hydrogen bond contained in the WT system.
Result: All the mutant systems had fewer hydrogen bonds than had the WT system; in particular, the V367F system only produced 14 hydrogen bonds.
Result: Although no hydrogen bond was formed at site 498 in the binding interface of both the V367F (Supplementary Figure S2B) and Q498A (Supplementary Figure S2C) systems, the hydrophobic interaction at this site was found to increase.
Result: Consistent with the result of our cell-cell fusion assay, recently, a study also found the enhanced affinity and infectivity of the V367F Spike mutant based on ELISA, SPR and the pseu
Potent prophylactic and therapeutic efficacy of recombinant human ACE2-Fc against SARS-CoV-2 infection in vivo.
Abstract: hACE2-Fc also neutralized various SARS-CoV-2 strains with enhanced infectivity including D614G and V367F mutations, as well as the emerging SARS-CoV-2 variants, B.1.1.7 (Alpha), B.1.351 (Beta), B.1.617.1 (Kappa), and B.1.617.2 (Delta), demonstrating its potent and broad-spectrum antiviral effects.
Method: In brief, HEK293 cells were co-transfected with reporter plasmid plenti-GFP-luc, packaging plasmid psPAX2, and coronavirus spike plasmid of interest (pcDNA3.1-SARS-CoV-S, pcDNA3.1-SARS-CoV-2-S, pcDNA3.1-SARS-CoV-2-S-D614G, pcDNA3.1-SARS-CoV-2-S-V367F, pcDNA3.1-B.1.1.7-S, pcDNA3.1-B.1.351-S, pcDNA3.1-B.1
Cross-neutralization of RBD mutant strains of SARS-CoV-2 by convalescent patient derived antibodies.
Result: As shown in Figure 4a, HTS0422, HTS0433 and HTS0446 bind with both wildtype and mutant (N501Y, W463R, N354D, V367F, both N354D and D364Y) RBD significantly.
Result: As shown in Figure 6a, the infection of mutants N354D, V367F and N354D/D364Y could be inhibited by all 4 antibodies.
Result: In this study, six different SARS-CoV-2 RBD mutants (N501Y, R408I, W463R, N354D, V367F an
Detection and characterization of the SARS-CoV-2 lineage B.1.526 in New York.
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: V367F
Mutational analysis in international isolates and drug repurposing against SARS-CoV-2 spike protein: molecular docking and simulation approach.
Result: The frequent mutations in different isolates are L5F, T22I, T29I, H49Y, L54F, V90F, S98F, S221L, S254F, V367F, A520S, T572I, D614G, H655Y, P809S, A879S, D936Y, A1020S, A1078S, and H1101Y.
Result: The other mutations, S98F mutation (USA, China, and Spai
Natto extract, a Japanese fermented soybean food, directly inhibits viral infections including SARS-CoV-2 in vitro.
PMID: 34271432
2021
Biochemical and biophysical research communications
Result: In addition, evolutionary analysis of the SARS-CoV-2 RBD protein indicated that V367F is one of important mutations for higher binding affinity toward ACE2 receptor.
Emerging mutation in SARS-CoV-2 spike: Widening distribution over time in different geographic areas.
Result: In addition, there were mutation types that have more than one case such as in Asia, the mutations A829T (n = 3), P25L (n = 2), V367F (n = 2), R682Q (n = 2), S13I (n = 2), and T22I (n = 2) while the other types have just one case.
Table: V367F
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.
V367F Mutation in SARS-CoV-2 Spike RBD Emerging during the Early Transmission Phase Enhances Viral Infectivity through Increased Human ACE2 Receptor Binding Affinity.
Figure: (A) Comparison of the binding affinity of prototype S protein and V367F mutant to human ACE2 receptor by ligand-receptor binding ELISA.
Figure: (B) Comparison of the binding affinity of prototype S protein and V367F mutant to human ACE2 protein by SPR.
Figure: (C) Quantification of the genome copy number of the V367F mutant versus the prototype using pseudovirus infection assay.
Figure: All 34 V367F mutants were included.
Figure: Experimental validation of the enhanced affinity and infectivity of the V367F mutant.
Figure: The relative fold increases of viruses infecting the cells are shown by the pseudoviral DNA copy number of the V367F mutant in both Vero and Caco-2 cell
SARS_CoV_2 mutation literature information.
PMID: 
2021
Infection and drug resistance
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