SARS_CoV_2 mutation literature information.


  Antigenicity comparison of SARS-CoV-2 Omicron sublineages with other variants contained multiple mutations in RBD.
 PMID: 35434713       2022       MedComm
Table: S477N


  Role of the Microbiome in the Pathogenesis of COVID-19.
 PMID: 35433495       2022       Frontiers in cellular and infection microbiology
Table: S477N


  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: The most prevalent D614G mutation and some mutations of interest (i.e., N501Y, L452R, K417N, N439K, S477N, S494P) were among the variants printed.
Discussion: The S variants tested here contain mutations that were selected from the COVID-19 virus mutation tracker database and literature, including known mutations like N501Y, L452R, K417N, N439K, S477N and S494P, and less publicized mutations (Figure S2).


  SARS-CoV-2 BA.1 variant is neutralized by vaccine booster-elicited serum, but evades most convalescent serum and therapeutic antibodies.
 PMID: 35380448       2022       Science translational medicine
Result: We compared the neutralization titers of these serum samples against pseudoviruses bearing spike proteins from the following variants: D614G, Omicron (A67V, del69-70, T95I, del142-144, Y145D, del211, L212I, ins214EPE, G339D, S371L, S373P, S375F, K417N, N440K, G446S, S477N, T478K, E484A, Q493R, G496S, Q498R,


  Mutational cascade of SARS-CoV-2 leading to evolution and emergence of omicron variant.
 PMID: 35367284       2022       Virus research
Table: S477N


  Multiorgan and Vascular Tropism of SARS-CoV-2.
 PMID: 35336922       2022       Viruses
Result: All SARS-CoV-2 genomes detected showed that the virus belonged to the clade 20A.EU2, with the presence of the characteristic S477N and the D614G mutations on the spike protein.


  Circulation of SARS-CoV-2 Variants among Children from November 2020 to January 2022 in Trieste (Italy).
 PMID: 35336187       2022       Microorganisms
Discussion: As for N439K, S477N occurs in the RBD region and seems to confer enhanced binding ability to the ACE2 receptor, but it does not seem to be associated with the loss of neutralizing activities of convalescent serum antibodies.
Discussion: In our cohort, and compared to the D614G strain, the S477N viral load was slightly lower, while no difference in the cl
Discussion: In our study, the S477N substitution was detected in one sample, with a frequency of 3.1%, resembling its frequency rate in Europe, which ranges from 4 to 7%.


  Omicron Variant of SARS-CoV-2 Virus: In Silico Evaluation of the Possible Impact on People Affected by Diabetes Mellitus.
 PMID: 35321335       2022       Frontiers in endocrinology
Discussion: This variation, together with several mutations on Spike-RBD that were linked to an increased affinity for ACE2 (such as S477N, Q498R, and N501Y), is predicted to contribute to an increase in the interactivity between Omicron-Spike-RBD and ACE2 in a hyperglycemic environment.


  Human serum from SARS-CoV-2-vaccinated and COVID-19 patients shows reduced binding to the RBD of SARS-CoV-2 Omicron variant.
 PMID: 35236358       2022       BMC medicine
Discussion: S477N, T478K, and E484A were initially at ~47% (status 2021-12-14, 2146 sequences), now instead above 88%, as N501Y (status 2022-02-07, 873.492 sequences).
Discussion: Several Omicron RBD mutations are assumed to increase the binding to ACE2: G339D, S477N, T478K, Q493K, and N501Y; others are proposed to be neutral: S371L, S373P, G446S, E484A, Q493R, and Q498R, or are assumed to reduce the binding to ACE2:  PMID: 35233566       2022       Research square
Abstract: To build an investigative framework, we have applied an unsupervised machine learning approach to 4296 Omicron viral genomes collected and deposited to GISAID as of December 14, 2021, and have identified a core haplotype of 28 polymutants (A67V, T95I, G339D, R346K, Introduction: Most of these mutations (G339D, N440K, G446S, S477N, T478K, E484A, Q493R, G496S, Q498R, N501Y, Y505H) present on the RBD surface.



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