ArticleNature structural & molecular biology2021
Effect of SARS-CoV-2 B.1.1.7 mutations on spike protein structure and function.
Article in Nature structural & molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.
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Who cites it
90 citing papers in PubMed, 168 citations in OpenAlex.
- Design and immunogenicity evaluation of pan-recombinant vaccines based on the consensus sequence of severe acute respiratory syndrome coronavirus-2 spike protein.Scientific reports · 2026Article
- Mutation and ACE2-induced allosteric network rewiring in Delta and Omicron SARS-CoV-2 spike proteins.Biophysical journal · 2026Article
- Mutation and ACE2-induced Allosteric Network Rewiring in Delta and Omicron SARS-CoV-2 Spike Proteins.bioRxiv : the preprint server for biology · 2025Article
- Profiling of sesquiterpenoid fractions fromBiomolecules & biomedicine · 2025Article
- Molecular basis of host recognition of human coronavirus 229E.Nature communications · 2025Article
- Identification of dominant peptide epitopes and antibody response to the spike protein of SARS-CoV-2.Frontiers in cellular and infection microbiology · 2025Article
- Dynamic expedition of leading mutations in SARS-CoV-2 spike glycoproteins.Computational and structural biotechnology journal · 2024Article
- Virion morphology and on-virus spike protein structures of diverse SARS-CoV-2 variants.The EMBO journal · 2024Article
- Current Updates on Variants of SARS-CoV- 2: Systematic Review.Health science reports · 2024Review
- Structure and inhibition of SARS-CoV-2 spike refolding in membranes.Science (New York, N.Y.) · 2024Article
- Enhancing Immune Responses against SARS-CoV-2 Variants in Aged Mice with INDUK: A Chimeric DNA Vaccine Encoding the Spike S1-TM Subunits.ACS omega · 2024Article
- Article
- Use of phase plate cryo-EM reveals conformation diversity of therapeutic IgG with 50 kDa Fab fragment resolved below 6 Å.Scientific reports · 2024Article
- Deciphering the free energy landscapes of SARS-CoV-2 wild type and Omicron variant interacting with human ACE2.The Journal of chemical physics · 2024Article
- Predicting the spread of SARS-CoV-2 variants: An artificial intelligence enabled early detection.PNAS nexus · 2024Article
- Structural proteins of human coronaviruses: what makes them different?Frontiers in cellular and infection microbiology · 2024Review
- Mutations accumulated in the Spike of SARS-CoV-2 Omicron allow for more efficient counteraction of the restriction factor BST2/Tetherin.PLoS pathogens · 2024Article
- Full-spike deep mutational scanning helps predict the evolutionary success of SARS-CoV-2 clades.bioRxiv : the preprint server for biology · 2023Article
- Development of AAV-delivered broadly neutralizing anti-human ACE2 antibodies against SARS-CoV-2 variants.Molecular therapy : the journal of the American Society of Gene Therapy · 2023Article
- In silico prediction of immune-escaping hot spots for future COVID-19 vaccine design.Scientific reports · 2023Article
30 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The B.1.1.7 variant of SARS-CoV-2 first detected in the UK harbors amino-acid substitutions and deletions in the spike protein that potentially enhance host angiotensin conversion enzyme 2 (ACE2) receptor binding and viral immune evasion. Here we report cryo-EM structures of the spike protein of B.1.1.7 in the apo and ACE2-bound forms. The apo form showed one or two receptor-binding domains (RBDs) in the open conformation, without populating the fully closed state. All three RBDs were engaged in ACE2 binding. The B.1.1.7-specific A570D mutation introduces a molecular switch that could modulate the opening and closing of the RBD. The N501Y mutation introduces a π-π interaction that enhances RBD binding to ACE2 and abolishes binding of a potent neutralizing antibody (nAb). Cryo-EM also revealed how a cocktail of two nAbs simultaneously bind to all three RBDs, and demonstrated the potency of the nAb cocktail to neutralize different SARS-CoV-2 pseudovirus strains, including B.1.1.7.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.