Result: 5): mutation S98F is located next to amino acid 69, which is deleted in variant B.1.1.7; substitution D574Y maps next to amino acid 570, which changes from alanine (A) to aspartic acid (D) in B.1.1.7 viruses; and mutations T478A, F490S, and S494P locate in the RBD, near amino acid 501, which changes from asparagine (N) to tyrosine (Y) in B.1.1.7.
Result: Most of these mutations have been found in clinical isolates from England, some of
Table: S494P
Discussion: Mutations T478A, F490S, and S494P, in particular, are located very close to amino acid 484, known to have an effect on virus antigenicity, as discussed above.
Rational optimization of a human neutralizing antibody of SARS-CoV-2.
PMID: 34147856
2021
Computers in biology and medicine
Table: S494P
Epitope Classification and RBD Binding Properties of Neutralizing Antibodies Against SARS-CoV-2 Variants of Concern.
Result: Additional conserved RBD contacts within the C2 NAb epitope suggests RBD variants G446V, L452R, and S4
Discussion: The current VoC include B.1.1.7-UK (N501Y, S494P*, E484K*), P.1-Japan/Brazil (K417N/T, E484K, N501Y), B.1.351-South Africa (K417N, E484K, N501Y) B.1.427/B.1.429-California (L452R), where amino acid changes in the SARS-CoV-2 S RBD of these VoC are listed in parentheses.
Simultaneous evaluation of antibodies that inhibit SARS-CoV-2 variants via multiplex assay.
Abstract: We describe the enhanced affinity of RBD variants N439K, S477N, Q493L, S494P, and N501Y to the ACE2 receptor and demonstrate the ability of this assay to bridge a major gap for SARS-CoV-2 research, informing selection of complementary monoclonal antibody candidates and the rapid identification of immune escape to emerging RBD variants following vaccination or natural infection.
Result: N439K and S494P had weakly enhanced overall affinity for ACE2, KD 25.2 nM and
Result: COVA2-15 and C135 demonstrated escape to G446V, while COVA2-15 demonstrated a loss of binding and inhibition to S494P.
Revealing the Threat of Emerging SARS-CoV-2 Mutations to Antibody Therapies.
Abstract: We unveil, for the first time, that high-frequency mutations R346K/S, N439K, G446V, L455F, V483F/A, F486L, F490L/S, Q493L, and S494P might compromise some of mAbs in clinical trials.
Emergence of the E484K mutation in SARS-COV-2-infected immunocompromised patients treated with bamlanivimab in Germany.
PMID: 34278371
2021
The Lancet regional health. Europe
Discussion: Gottlieb and colleagues reported an emergence of escape mutants (E484K; E484Q; F490S and S494P) in 28/297 (9 4%) patients who received bamlanivimab monotherapy and even in 7/145 (4 8%) of patients receiving placebo in the phase 2/3 BLAZE-1 trial.
Mutational analysis in international isolates and drug repurposing against SARS-CoV-2 spike protein: molecular docking and simulation approach.
Figure: (F, H) Paired analysis of neutralizing activity of convalescent sera (F) or post-vaccination sera (H) against WT vs S494P,
Figure: (F-I) Neutralization assays were performed against pseudoviruses displaying WT or S494P spike mutants, in the presence of serial dilutions of convalescent sera (F, G) or post-vaccination sera 1 month after the first and the second rounds of vaccination (H, I).
Discussion: Of note, current prevalence of B.1.351 and of P.1 is 1.9% and 0.47%, respectively, being in the same range as S494P.
Discussion: The mutation S494P has been found in nature with a prevalence of 0.81% of all sequenced genomes (March 2021, S1 Fig) and has already been observed in combination with mutation E484K (reported on the 22nd of October 2020).
Neutralizing Activity of Sera from Sputnik V-Vaccinated People against Variants of Concern (VOC: B.1.1.7, B.1.351, P.1, B.1.617.2, B.1.617.3) and Moscow Endemic SARS-CoV-2 Variants.
Introduction: These mutations are likely to include K417N, L452R, E484K, S494P and N501Y/T, based on molecular dynamics data.
Result: The RBD variability data obtained for SARS-CoV-2 variants from Moscow patients (Figure 2, dashed lines) are generally consistent with the variability data for Russian sequences available in GISAID (Figure 2, solid lines and Figure S1) showing increasing prevalence of S477N, A522S, E484K, N501Y, T385I, S494P, N439K, K417N, T487K
Acquisition of the L452R Mutation in the ACE2-Binding Interface of Spike Protein Triggers Recent Massive Expansion of SARS-CoV-2 Variants.
PMID: 34379531
2021
Journal of clinical microbiology
SARS_CoV_2 mutation literature information.
PMID: 
2021
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