A bioluminescent and homogeneous SARS-CoV-2 spike RBD and hACE2 interaction assay for antiviral screening and monitoring patient neutralizing antibody levels.
Method: The following proteins were purchased from Sino Biological (Beijing, China): SARS-CoV-2 recombinant Spike RBD wild type, RBD (S477N), RBD (Y453F), RBD (K458R), RBD (F342L), RBD (
Result: However, RBD mutants S477N, Y453F and N501Y showed higher apparent affinity toward hACE2 as evidenced by fourfold, eightfold, and tenfold reductions in their respective IC50 values compared to wild type RBD.
Exploiting genomic surveillance to map the spatio-temporal dispersal of SARS-CoV-2 spike mutations in Belgium across 2020.
Method: In particular, we targeted three specific mutations in the spike protein (S98F, A222V, and S477N) due to their rapid expansion and dissemination across Europe during the summer months.
Result: Finally, the S477N spike mutation was first detected at the end of the summer and displays moderate regional circulation and detection frequency (13.5%).
Result: It has recently been reported that S477N might strengthen the binding of the SARS-COV-2 spike with the human ACE2 receptor, which could potentially be associated with enhanced viral transmissibility.
Figure: We report the estimated temporal evolution of the frequency of the main spike mutations in the pr
Receptor binding, immune escape, and protein stability direct the natural selection of SARS-CoV-2 variants.
PMID: 34543625
2021
The Journal of biological chemistry
Abstract: Compared with the wildtype, four mutants (K417N, Y453F, N501Y, and K417T/E484K/N501Y) had weaker affinity for the CC12.1 antibody, whereas two (S477N and S494P) had similar affinity, and two (T478I and E484K) had stronger affinity than the wildtype.
Abstract: Of the eight best-expressed mutants, two (N501Y and K417T/E484K/N501Y) showed stronger affinity to angiotensin-converting enzyme 2 compared with the wildtype, whereas four (Y453F,
Mutations of SARS-CoV-2 RBD May Alter Its Molecular Structure to Improve Its Infection Efficiency.
Result: Additionally, S477N and L452R showed different loop conformers at loop 457-467 (a flexible loop) of RBM, while N501Y, E484K, and N439K showed similar conformers in the same region during the simulations (Figure 3b).
Result: As anticipated, the mutation of S477N and E484K would not form hydrogen bonds since their mutation sites are located in the binding interacting loop (Figure 2b).
Result: C-alpha root mean square deviation (C-alpha RMSD) was assessed during the 100-ns MD simulation runs for WT RBD and N501Y, L452R, S477N, N439K, and
Emergence and spread of SARS-CoV-2 lineage B.1.620 with variant of concern-like mutations and deletions.
Method: Prior to official lineage designation as B.1.620, most of its genomes could be identified by the presence of spike protein E484K and S477N mutations and the HV69/70Delta deletion.
Method: Searching GISAID for mutations E484K, S477N and HV69/70Delta, which are found in numerous VOCs individually but not in combination, identified additional genomes that contained other mutations and deletions found in B.1.620.
Method: This study was initiated upon detection of SARS-CoV-2 strains in Lithuania bearing spike protein amino acid substitutions E484K, S477N and numerous B.1.1.7-like (HV69/70Delta and Y144Delta) and B.1.351-like (LLA241/243Delta) deletions, amongst others.
Method: We have modelled
Variants of SARS-CoV-2, their effects on infection, transmission and neutralization by vaccine-induced antibodies.
PMID: 34604978
2021
European review for medical and pharmacological sciences
Abstract: S477N, E484K, Q677H, E484Q, L452R, K417T, K417N and N501Y.
Spread of Mink SARS-CoV-2 Variants in Humans: A Model of Sarbecovirus Interspecies Evolution.
Introduction: Based on the 3D modeling of the SARS-CoV-2 spike-human ACE2 interactions we visualized the location of amino acids described as major mutation sites in the SARS-CoV-2 variants infecting humans, i.e., the S477N, E484K, and N501Y/T mutations known to characterize the Marseille-4 variant (France), the 20I/501Y.V1 variant (United Kingdom), and the 20H/501Y.V2 variant (South Africa) (Figure 8A, left panel).
Evaluation of the clinical and analytical performance of the Seegene allplex SARS-CoV-2 variants I assay for the detection of variants of concern (VOC) and variants of interests (VOI).
SARS-CoV-2 Virus-Host Interaction: Currently Available Structures and Implications of Variant Emergence on Infectivity and Immune Response.
PMID: 34639178
2021
International journal of molecular sciences
Discussion: The mutated RBD (PDB 7BH9) presents, among others, eight amino acid changes actively engaged in the interaction with hACE2, namely V445K, N460K, I468T, T470M, S477N, E484K, Q498R and N501Y.
Ten emerging SARS-CoV-2 spike variants exhibit variable infectivity, animal tropism, and antibody neutralization.
Abstract: RBD amino acid mutations comprising K417T/N, L452R, Y453F, S477N, E484K, and N501Y cause significant immune escape from 11 of 13 monoclonal antibodies.
Result: Furthermore, the variant B.1.429 and L452R single-mutation strain
Figure: b Structural modelling of the K417N/T, L452R, Y453F, S477N, E484K and N501Y mutations, based on 7chh for X593, RBD-7B8 for 7B8, RBD-Ab1 for 10D 12, and 7c01 for CB6.
SARS_CoV_2 mutation literature information.
PMID: 
2021
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