Introduction: The variants A222V (clade 20A.EU1) and S477N (clade 20A.EU2) emerged in the summer of 2020 in Spain and have rapidly shown diffusion within Europe.
Ongoing global and regional adaptive evolution of SARS-CoV-2.
Discussion: Other common mutations in the spike (S) protein, including A222V (C22227T), L81S (C21614T), and S477N (G22992A), are co-occurred with D614G in 100,401 sequences (21.8%), 45,943 sequences (10%) and 23,426 sequences (5.1%), respectively (Covid19 CG data: https://covidcg.org/?tab=group).
B.1.526 SARS-CoV-2 Variants Identified in New York City are Neutralized by Vaccine-Elicited and Therapeutic Monoclonal Antibodies.
Abstract: Two versions of the variant were identified, both with the prevalent D614G mutation in the spike protein, together with four novel point mutations and with an E484K or S477N mutation in the receptor-binding domain, raising concerns of possible resistance to vaccine-elicited and therapeutic antibodies.
Abstract: We report that convalescent-phase sera and vaccine-elicited antibodies retain full neutralizing titer against the S477N B.1.526 variant and neutralize the Table: S477N
Figure: The locations of the mutations in the two B.1.526 spike proteins are diagrammed below with the distinguishing E484K and S477N mutations in bold.
Conformational Variability Correlation Prediction of Transmissibility and Neutralization Escape Ability for Multiple Mutation SARS-CoV-2 Strains using SSSCPreds.
Abstract: The conformational variability of the mutation sites for B.1.617.2 (Delta), B.1.617.1 (kappa), B.1.427/429 (epsilon), P.1 (gamma), B.1.351 (beta), B.1.1.7 (alpha), S477N, and the wild-type strain has been assessed using a deep neural-network-based prediction program of conformational flexibility or rigidity in proteins (SSSCPreds).
Conclusion: In conclusion, the conformational variability of the mutation sites for B.1.617.2, B.1.617.1, B.1.427/429, P.1, B.1.351,
Introduction: As for the receptor-binding motif (RBM) of spike protein, before B.1.1.7, B.1.351, and P.1, the mutation of S477N has expanded in Australia and in Europe but has not led to an extension of the pandemic ().
Figure: Sequence flexibility/rigidity map of the RBM regions of B.1.617.2,B.1.617.1, B.1.427/429, P.1, B.1.351, B.1.1.7, S477N, and the wild-typestrain.
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.
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, N501T, and Y508H mutations.
Result: The study of the neutralizing activity of Sputnik V induced sera against SARS-CoV-2 variants showed no significant differences in the levels of VNT for B.1.1.1, B.1.1.141 (T
Molecular Evolution and Epidemiological Characteristics of SARS COV-2 in (Northwestern) Poland.
Result: The first one was DeltaH69V70 and N439 in lineage B.1.258 (20A), then D138Y with S477N observed for B.1.1.317 (20B), and finally A222V and L18F in the B.1.177 (20E EU1) strains.
Detection and characterization of the SARS-CoV-2 lineage B.1.526 in New York.
Result: One of these sub-lineages defined by spike mutations S477N, V701A, and Q957R, has been designated B.1.526.2, but for the purposes of characterizing epidemic and phylodynamic growth of this variant, we combine B.1.526 and B.1.526.2.
Result: Regarding four of the spike mutations prevalent in this lineage: (1) E484K is known to attenuate neutralization of multiple anti-SARS-CoV-2 antibodies, particularly those found in class 2 anti-RBD neutralizing antibodies, and is also present in variants B.1.351 and P.1/B.1.1.248, (2) D253G has been reported as an escape mutation from antibodies against the N-terminal domain, (3) S477N has been identif
SARS-CoV-2 receptor-binding mutations and antibody contact sites.
Abstract: The high frequency S477N mutation is present in 6.7% of all SARS-CoV-2 sequences, co-occurs with D614G, and is currently present in 14 countries.
Abstract: We report high frequency mutations with improved binding affinity to ACE2 including S477N, N439K, V367F, and N501Y and address the potential impact of RBD mutations on antibody binding.
Conclusion: In conclusion,
Introduction: We found four high frequency variants with improved binding to ACE2:S477N, N439K, V367F, and N501Y and cross-referenced antibody interaction data with RBD mutations.
SARS-CoV-2 variant prediction and antiviral drug design are enabled by RBD in vitro evolution.
Abstract: We found that mutations present in more transmissible viruses (S477N, E484K and N501Y) were preferentially selected in our high-throughput screen.
SARS_CoV_2 mutation literature information.
PMID: 
2021
Journal of virology
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