ArticleCell2020
Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies.
Article in Cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 329 papers, 2 of them syntheses that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
329 citing papers in PubMed, 2 syntheses or guidelines pooled it, 651 citations in OpenAlex.
- SARS-CoV-2-neutralising monoclonal antibodies to prevent COVID-19.The Cochrane database of systematic reviews · 2022Pooled it
- Outlook of therapeutic and diagnostic competency of nanobodies against SARS-CoV-2: A systematic review.Analytical biochemistry · 2022Pooled it
- Article
- ACE2-fused nanobody targeting a cryptic RBD epitope broadly neutralizes SARS-like viruses.Journal of virology · 2026Article
- A Generative Neuro-Symbolic AI for Protein Sequence Design.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Scalable and sustainable manufacturing of functional DNA nanoassemblies via self-folding circular single-stranded DNA.Nature communications · 2026Article
- Multifunctional ACE2-nanobody fusion design for pan-specific neutralization and cardiovascular protection in SARS coronavirus infection.Antimicrobial agents and chemotherapy · 2026Article
- Structural Basis of MERS-CoV Receptor Interactions and Antibody Neutralisations.Reviews in medical virology · 2026Review
- Decoding antibody response to MERS-CoV in wild dromedary camels.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- AlphaBind, a domain-specific model to predict and optimize antibody-antigen binding affinity.mAbs · 2025Article
- Article
- Review
- Pharmacoinformatics-based screening and construction of a neutralizing anti-SARS-CoV-2 camelidae nanobody drug conjugate.Molecular diversity · 2025Article
- Article
- Optimization of a sarbecovirus llama nanobody-antigen binding interface via a combined computational and phage display protein engineering approach.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Identification of a nanobody able to catalyze the destruction of the spike-trimer of SARS-CoV-2.Frontiers of medicine · 2025Article
- Ultrapotent SARS coronavirus-neutralizing single-domain antibodies that clamp the spike at its base.Nature communications · 2025Article
- Optimization of synthetic human VProtein science : a publication of the Protein Society · 2025Article
- Article
- A bivalent spike-targeting nanobody with anti-sarbecovirus activity.Journal of nanobiotechnology · 2025Article
269 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
- Erratum issued
Authors and funding
16 authors at 5 institutions in 3 countries.
Funding
Abstract
Coronaviruses make use of a large envelope protein called spike (S) to engage host cell receptors and catalyze membrane fusion. Because of the vital role that these S proteins play, they represent a vulnerable target for the development of therapeutics. Here, we describe the isolation of single-domain antibodies (VHHs) from a llama immunized with prefusion-stabilized coronavirus spikes. These VHHs neutralize MERS-CoV or SARS-CoV-1 S pseudotyped viruses, respectively. Crystal structures of these VHHs bound to their respective viral targets reveal two distinct epitopes, but both VHHs interfere with receptor binding. We also show cross-reactivity between the SARS-CoV-1 S-directed VHH and SARS-CoV-2 S and demonstrate that this cross-reactive VHH neutralizes SARS-CoV-2 S pseudotyped viruses as a bivalent human IgG Fc-fusion. These data provide a molecular basis for the neutralization of pathogenic betacoronaviruses by VHHs and suggest that these molecules may serve as useful therapeutics during coronavirus outbreaks.
Indexed as
Identifiers
What OpenQuestion holds
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.