SARS_CoV_2 mutation literature information.


  Characteristic analysis of Omicron-included SARS-CoV-2 variants of concern.
 PMID: 35434714       2022       MedComm
Discussion: The same spike proteins, K444E, G446 V, L452R, and F490S, can also evade serum neutralization.


  Inhibitor screening using microarray identifies the high capacity of neutralizing antibodies to Spike variants in SARS-CoV-2 infection and vaccination.
 PMID: 35401825       2022       Theranostics
Result: Notably, structural analyses show that 5 escape mutations (K417N/E484K/N501Y, G446V, F456E, N487R, F490L) are located within the interface of RBD-ACE2 interaction, indicating that this RBD subdomain is important in neutralizing SARS-CoV-2 infection.
Result: Using statistical analysis, the neutralization of convalescent serum NAbs to eight mutated proteins was significantly decreased, including 4 known escape mutations [K417N, G446V, F490L, K417N/E484K/N501Y<


  Emerging Vaccine-Breakthrough SARS-CoV-2 Variants.
 PMID: 35133792       2022       ACS infectious diseases
Result: Notably, comutaion set [G446V, L452R, T478K] in the UK with BFE change of 1.733 kcal/mol and 46 antibody disruption counts appears to be a dangerous set of comutations that may affect the infectivity and vaccine/antibodies efficacy shortly.


  E484K and N501Y SARS-CoV 2 spike mutants Increase ACE2 recognition but reduce affinity for neutralizing antibody.
 PMID: 34915409       2022       International immunopharmacology
Introduction: G446V RBD mutation was reported to reduce ACE2 binding affinities, but S477N mutation strengthen the binding between SARS-CoV2 spike RBD and hACE2.
Introduction: On the otherhand, G446V, S477N, G485R, and F490S RBD mutants demonstrated ~3-5 fold decrease in neutralization titer for few sera.
Table: G446V


  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: G446V


  Mutational analysis in international isolates and drug repurposing against SARS-CoV-2 spike protein: molecular docking and simulation approach.
 PMID: 34307771       2021       Virusdisease
Table: G446V


  Emerging vaccine-breakthrough SARS-CoV-2 variants.
 PMID: 34518803       2021       ArXiv
Result: Notably, co-mutaion set [G446V, L452R, T478K] in the UK with BFE change of 1.733 kcal/mol and 46 antibody disruption counts appears to be a dangerous set of co-mutations that may affect the infectivity and vaccine/antibodies efficacy shortly.


  SARS-CoV-2 Variants, RBD Mutations, Binding Affinity, and Antibody Escape.
 PMID: 34829998       2021       International journal of molecular sciences
Introduction: There have been a number of missense mutations observed in the receptor-binding domain (RBD) of the SARS-CoV-2 S protein, which have presented in one or more of the VOCs, including the N440K, G446V, L452R, Y453F, E484Q, F490S, N501Y, N501S, E484K, and K417N, most of which are located at the RBD-ACE2 interface.


  The Development of SARS-CoV-2 Variants: The Gene Makes the Disease.
 PMID: 34940505       2021       Journal of developmental biology
Introduction: Mutation Y453F, along with N439K, G446V, K444E, and S477N, among others, which are located at the interface between the S1 and ACE2, have been shown to partially interfere with antibody binding and neutralization.


  Phylodynamic Pattern of Genetic Clusters, Paradigm Shift on Spatio-Temporal Distribution of Clades, and Impact of Spike Glycoprotein Mutations of SARS-CoV-2 Isolates from India.
 PMID: 35017872       2021       Journal of global infectious diseases
Result: Among the mutations in RBD, R346K, N440K, G446V, N450K, V483F, E484K, E484Q, F490S and S494P also showed change in ACE2 binding to the extent of 75% to 90%.



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