Natto extract, a Japanese fermented soybean food, directly inhibits viral infections including SARS-CoV-2 in vitro.
PMID: 34271432
2021
Biochemical and biophysical research communications
Abstract: In addition, RBD protein carrying a point mutation (UK variant N501Y) was also degraded by the natto extract.
Method: We also used UK variant N501Y RBD-His recombinant protein (Sino Biological, PA, USA).
Figure: (C) The recombinant RBD protein of SARS-CoV-2 carrying a point mutation (N501Y) was incubated with the heated or unheated natto extract.
Figure: Lane 1: protein marker, Lane 2: RBD protein (N501Y) treated with PBS, Lane 3: RBD protein (N501Y) treated with unheated-natto extract, Lane 4: RBD protein (N501Y) treated with heated
Estimating COVID-19 cases infected with the variant alpha (VOC 202012/01): an analysis of screening data in Tokyo, January-March 2021.
PMID: 34273991
2021
Theoretical biology & medical modelling
Abstract: BACKGROUND: In Japan, a part of confirmed patients' samples have been screened for the variant of concern (VOC), including the variant alpha with N501Y mutation.
Introduction: Japan intensified sequencing virus samples from late December both at border quarantine station and domestic testing centers, and also devised a real-time polymerase chain reaction (rt-PCR) technique to detect N501Y mutation as the screening method in each prefecture.
Introduction: New and Emerging Respiratory Virus Threats Advisory Group (NERVTAG) in the United Kingdom (UK) identified the common mutation N501Y in the variant alpha.
Method: It should be noted that week t in our study represents the week of screening testing for N501Y mutation, no
Method: confirmed s = 2 weeks earlier than screening for N501Y).
Emergence in southern France of a new SARS-CoV-2 variant harbouring both N501Y and E484K substitutions in the spike protein.
PMID: 34274369
2021
Journal of virological methods
Abstract: The emergence of SARS-CoV-2 mutations resulting in the S protein amino-acid substitutions N501Y and
Introduction: In all of these 3 VOCs, the N501Y amino-acid substitution (change of asparagine to tyrosine) is present at the position 501 of the S-protein (receptor-binding domain), which confers enhanced affinity for receptor binding.
Introduction: In conclusion, the typing real-time RT-PCR assay developed herein is able to accurately identify the mutations associated with the E484K and N501Y phenotypes of SARS-CoV-2 S protein, considered as MOCs.
Introduction: before the emergence of E484K and N501Y amino-acid substitutions in Greece were included.
SARS-CoV-2 testing and sequencing for international arrivals reveals significant cross border transmission of high risk variants into the United Kingdom.
Introduction: 69-70del is thought to lead to increased transmissibility in combination with N501Y.
Introduction: N501Y is found in the receptor binding domain (RBD) of the spike protein and has been shown to increase its binding affinity to human angiotensin-concerting enzyme 2 (ACE2), the virus' primary mode of entry into human cells.
Introduction: Indeed, evidence suggests both the Moderna and Pfizer vaccines are less effective at neutralising viruses with these mutations and of 17 vaccine-elicited antibodies tested, 9 were at least 10 times less effective against pseudotyped viruses containing E484K, 5 against K417N and 4 against N501Y.
Introduction: The combination of nearby
Efficient Inhibition of SARS-CoV-2 Using Chimeric Antisense Oligonucleotides through RNase L Activation*.
PMID: 34278671
2021
Angewandte Chemie (International ed. in English)
Introduction: Mutations DeltaH69/DeltaV70 and N501Y on the spike protein of SARS-CoV-2 have been reported to cause S-gene target failure (SGTF) and greatly increase viral transmissibility.
Introduction: One of these chimeras also effectively inhibited three SARS-CoV-2 pseudovirus mutants, including N501Y, DeltaH69/DeltaV70, and the recently discovered dual-site mutations with higher transmission ability.
Introduction: Since mutation sites on S-RNA corresponding to N501Y and DeltaH69/DeltaV70 are not overlaid with targeted region of Chimera-S4, unaffected high potent inhibition of these mutants was still successfully achieved.
Introduction: This chimeric sequence still showed robust inhibiting capability toward three highly transmissible SARS-CoV-2 mutants involving
Evolutionary Tracking of SARS-CoV-2 Genetic Variants Highlights an Intricate Balance of Stabilizing and Destabilizing Mutations.
A Simple Reverse Transcriptase PCR Melting-Temperature Assay To Rapidly Screen for Widely Circulating SARS-CoV-2 Variants.
PMID: 34288729
2021
Journal of clinical microbiology
Method: A 250-nucleotide region around the N501Y (A23063T) and E484K (G23012A) positions in the reference strain (GenBank accession number MN908947) was selected and used to identify the corresponding regions in the GISAID data set using BLAST.
Table: N501Y
Figure: Prevalence of N501Y variant strains among the tested sample set over time.
Figure: The proportion of N501Y and E484K variants is shown for samples obtained during the periods of October to November (n = 9 tested with SMB-501/n = 3 tested with SMB-484), January (n = 16/n = 12), February (n = 15/n = 9), and the first week of March (n = 6/n = 2).
Discussion: Although in this study we have proposed the use of a combination of
A selective sweep in the Spike gene has driven SARS-CoV-2 human adaptation.
Method: Functional ELISA was performed by Sino Biological (Wayne, PA) using purified RBD from WT (Cat: 40592-V08H), A372T (Cat: 40592-V08H36), and N501Y (Cat: 40592-V08H82).
Result: EC50 values compared directly showed robust differences between the WT and A372T or N501Y (Figure 3B; both p < 0.0001 by one-way
Table: N501Y
Figure: Plates were coated with recombinant human ACE2 receptor (2 mug/mL at 100 muL/well) and then probed with varying concentrations (0.256-4000 ng/mL) of purified RBDs from WT SARS-CoV-2 (S A372), A372T, and N501Y (positive control).
Ongoing global and regional adaptive evolution of SARS-CoV-2.
Result: N501Y is among the 22 strongest candidates for positive selection and has been demonstrated to escape neutralizing antibodies.
Result: In particular, S N501Y and N S235F are both signature mutations for variants B.1.1.7 and B.1.1.7_E484K (SI Appendix, Table S4, List 2), and this pair is in the top 25% of cooccurring pairs in our network, ranked by lowest probability of random cooccurrence.
Result: Of greatest concern is perhaps N501Y.
Result: Three of these signature mutations pass the strict criteria for positive selection:S N501Y, S S477N, and
Neutralization of SARS-CoV-2 by highly potent, hyperthermostable, and mutation-tolerant nanobodies.
Abstract: We constructed nanobody tandems and identified nanobody monomers that tolerate the K417N/T, E484K, N501Y, and L452R immune-escape mutations found in the Alpha, Beta, Gamma, Epsilon, Iota, and Delta/Kappa lineages.
SARS_CoV_2 mutation literature information.
PMID: 
2021
Biochemical and biophysical research communications
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