Neutralisation sensitivity of the SARS-CoV-2 omicron (B.1.1.529) variant: a cross-sectional study.
PMID: 35305699
2022
The Lancet. Infectious diseases
Introduction: Deep mutational scanning data suggest that E484A and K417N, in addition to G446S and Q493R (which are not present in other variants of concern) are the largest contributors to the resistance profile of the omicron variant.
A Detailed Overview of Immune Escape, Antibody Escape, Partial Vaccine Escape of SARS-CoV-2 and Their Emerging Variants With Escape Mutations.
Method: We therefore generated and used an Omicron Spike bearing the Q493R mutation for the full manuscript (Figures 1 and 2 and Figure S1).
Discussion: As i
Discussion: Of note, the sequence initially released for the Omicron Spike contained the Q493K substitution, but was then corrected to Q493R.
Discussion: Previous in vitro studies already showed the association of some of these mutations with increased infectivity, ACE2 interaction (N501Y, P681H), or immune evasion (K417N, N440K, G446S, S477N, E484A/K, Q493R).
Allosteric Determinants of the SARS-CoV-2 Spike Protein Binding with Nanobodies: Examining Mechanisms of Mutational Escape and Sensitivity of the Omicron Variant.
PMID: 35216287
2022
International journal of molecular sciences
Result: According to the recent study, the Omicron variant can escape the neutralization of many monoclonal antibodies, where the K417N, Q493R, and E484A Omicron mutations affect the recognition of class 1 and 2 antibodies targeting the ACE2 binding epitope.
Result: For VHH E binding, the large binding affinity loss resulted from E484A, Q493R, G496S, and N501Y mutations (Figure 7C,D).
Result: Hence, multiple Omicron RBD mutations (such as Q493R, G496S, Q498R, N501Y, Y505H) may have a measurable effect on allosteric couplings i
Spike Gene Evolution and Immune Escape Mutations in Patients with Mild or Moderate Forms of COVID-19 and Treated with Monoclonal Antibodies Therapies.
Abstract: Four out of the 13 patients acquired a mutation during follow-up; two mutations (G1204E and E406G) appeared as a mixture without clinical impact, while the Q493R mutation emerged in two patients (one receiving bamlanivimab and one receiving bamlanivimab/etesevimab) with fatal outcomes.
Introduction: Some cases of Q493R mutations following bamlanivimab/etesevimab administration were also reported in the literature and are associated with a reduced viral clearance and, in some patients, with fatal outcome.
Result: All the patients recovered from COVID-19, except the two patients with the Q493R-acquired mutations.
Result: In total, five mutations (A67V, E406E/G, PMID: 35208920
2022
Microorganisms
Result: In addition, fifteen other substitutions affect the spike protein including Q954H, N764K, H655Y, K417N, G339D, N211K, Q493R, S371L, S373P, S375F, S477N, T478K, E484A, N440K and G446S were detected as the most frequent mutation events in more than 84% of total genomes.
mRNA-1273 Vaccine-elicited Neutralization of SARS-CoV-2 Omicron in Adolescents and Children.
Abstract: We report that the Omicron brings an enhanced RBD-ACE2 interface through N501Y, Q493K/R, and T478K mutations; the changes further lead to unique interaction patterns, reminiscing the features of previously dominated variants, Alpha (N501Y) and Delta (L452R and T478K).
Introduction: Our study reveals that the Omicron mutations lead to an enhancement of binding between RBD and ACE2 by forming unique interaction patterns, which are caused mainly by N501Y, Q493K/R, and T478K mutations.
Method: To improve statistical results, 20 independent simulation runs of two Omicron variants
Divergent SARS-CoV-2 Omicron-reactive T and B cell responses in COVID-19 vaccine recipients.
Introduction: However, substitutions of Y505H and K417N abolished three hydrogen bonds formed with K75, D31 and E104 from the heavy chain complementarity-determining regions (HCDRs), leading to conformational shifts in HCDR3 and the RBM tip (residues 470-490), which further perturbed six hydrogen bonds built by Y473, A475, S477, T478 and Q493 from WT RBD with T105, C107, A56, G55 and D109 from the HCDRs, albeit with an extra hydrogen bond established by the mutation Q493R and G55 from HCDR2 for Omicron (Extended Data.
Introduction: The pattern of some of these alterations, similar to the those noted in previous VOCs, such as Delta69-70 in Alpha (B.1.1.7), N501Y in Alpha, Beta and Gamma (P.1), and P681H in Alpha and Delta (B.1.617.2), are associated with enhanced transmissibility, wh
SARS_CoV_2 mutation literature information.
PMID: 
2022
The Lancet. Infectious diseases
Browser Board
Co-occurred Entities
Filtrator
ViMRT