ArticleNature structural & molecular biology2021
Structural basis for broad coronavirus neutralization.
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 157 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
157 citing papers in PubMed, 208 citations in OpenAlex.
- Structural basis of diverse antibody recognition of conserved coronavirus spike S2 epitopes that contribute to protective immunity.bioRxiv : the preprint server for biology · 2026Article
- Identification of Conserved B-Cell Epitope Candidates Associated with Neutralizing Activity of Bovine Coronavirus Spike Protein.Animals : an open access journal from MDPI · 2026Article
- Article
- Directed evolution of a stem-helix-targeting antibody enables MERS-CoV cross-neutralization through enhanced binding affinity.PLoS pathogens · 2026Article
- Broad Neutralizing Antibodies Against SARS-CoV-2: Current Progress and Engineering Strategies.Viruses · 2026Review
- TMPRSS2-mediated coronavirus spike activation and inhibition.Nature structural & molecular biology · 2026Article
- Repeated COVID-19 vaccine boosters elicit variant-specific memory B cells in humans.Cell reports · 2026Article
- EMoMiS: A pipeline for epitope-based molecular mimicry search in protein structures with potential applications to SARS-CoV-2.Computational and structural biotechnology journal · 2026Article
- Unconventional linkers facilitate potent stabilized coronavirus stem antibody responses following nanoparticle vaccination.bioRxiv : the preprint server for biology · 2025Article
- Structural Insights into the SARS-CoV-2 Spike Protein and Its Implications for Antibody Resistance.Biomolecules · 2025Review
- Directed evolution of a stem-helix-targeting antibody enables MERS-CoV cross-neutralization through enhanced binding affinity.bioRxiv : the preprint server for biology · 2025Article
- Article
- Designed miniproteins potently inhibit and protect against MERS-CoV.Cell reports · 2025Article
- Article
- Review
- Unveiling the structural spectrum of SARS-CoV-2 fusion by in situ cryo-ET.Nature communications · 2025Article
- A global collaboration for systematic analysis of broad-ranging antibodies against the SARS-CoV-2 spike protein.Cell reports · 2025Article
- Structural basis and mode of action for two broadly neutralizing nanobodies targeting the highly conserved spike stem-helix of sarbecoviruses including SARS-CoV-2 and its variants.PLoS pathogens · 2025Article
- RBD-depleted SARS-CoV-2 spike generates protective immunity in cynomolgus macaques.NPJ vaccines · 2025Article
- Molecular basis of convergent evolution of ACE2 receptor utilization among HKU5 coronaviruses.Cell · 2025Article
97 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
15 authors at 5 institutions in 5 countries.
Funding
Abstract
Three highly pathogenic β-coronaviruses have crossed the animal-to-human species barrier in the past two decades: SARS-CoV, MERS-CoV and SARS-CoV-2. To evaluate the possibility of identifying antibodies with broad neutralizing activity, we isolated a monoclonal antibody, termed B6, that cross-reacts with eight β-coronavirus spike glycoproteins, including all five human-infecting β-coronaviruses. B6 broadly neutralizes entry of pseudotyped viruses from lineages A and C, but not from lineage B, and the latter includes SARS-CoV and SARS-CoV-2. Cryo-EM, X-ray crystallography and membrane fusion assays reveal that B6 binds to a conserved cryptic epitope located in the fusion machinery. The data indicate that antibody binding sterically interferes with the spike conformational changes leading to membrane fusion. Our data provide a structural framework explaining B6 cross-reactivity with β-coronaviruses from three lineages, along with a proof of concept for antibody-mediated broad coronavirus neutralization elicited through vaccination. This study unveils an unexpected target for next-generation structure-guided design of a pan-β-coronavirus vaccine.
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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.