ArticleProceedings of the National Academy of Sciences of the United States of America2017
Antibody-induced uncoating of human rhinovirus B14.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
36 citing papers in PubMed, 61 citations in OpenAlex.
- Cross-Neutralizing and Broadly Neutralizing Human Antibodies Against Nonenveloped Viruses.European journal of immunology · 2026Review
- Different mechanisms for human rhinovirus survival in the presence of deleterious amino acid substitutions at virion protein-protein or RNA-protein interfaces.Journal of virology · 2026Article
- Optimized Propagation and Purification Protocols for Large-Scale Production of Rhinovirus C.Viruses · 2026Article
- Neutralizing Antibodies vs. Viruses: Interacting Mechanisms and Escape Tactics.Microorganisms · 2025Review
- A single residue switch mediates the broad neutralization of Rotaviruses.Nature communications · 2025Article
- Fc-FcγR interactions during infections: From neutralizing antibodies to antibody-dependent enhancement.Immunological reviews · 2024Review
- Discovery, recognized antigenic structures, and evolution of cross-serotype broadly neutralizing antibodies from porcine B-cell repertoires against foot-and-mouth disease virus.PLoS pathogens · 2024Article
- Neutralizing antibody landscape of the non-polio Enteroviruses and future strategy.Frontiers in immunology · 2024Review
- Molecular Determinants of Human Rhinovirus Infection, Assembly, and Conformational Stability at Capsid Protein Interfaces.Journal of virology · 2022Article
- Review
- Structures of Foot-and-Mouth Disease Virus with Bovine Neutralizing Antibodies Reveal the Determinant of Intraserotype Cross-Neutralization.Journal of virology · 2021Article
- Functional and structural characterization of a two-MAb cocktail for delayed treatment of enterovirus D68 infections.Nature communications · 2021Article
- ICAM-1 induced rearrangements of capsid and genome prime rhinovirus 14 for activation and uncoating.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- High resolution single particle Cryo-EM refinement using JSPR.Progress in biophysics and molecular biology · 2021Review
- Mechanisms of Rhinovirus Neutralisation by Antibodies.Viruses · 2021Review
- Molecular basis for protein-protein interactions.Beilstein journal of organic chemistry · 2021Review
- Article
- Serotype specific epitopes identified by neutralizing antibodies underpin immunogenic differences in Enterovirus B.Nature communications · 2020Article
- ELISA-Based Assay for Studying Major and Minor Group Rhinovirus-Receptor Interactions.Vaccines · 2020Article
- The Dynamic Life of Virus Capsids.Viruses · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Rhinoviruses (RVs) are the major causes of common colds in humans. They have a nonenveloped, icosahedral capsid surrounding a positive-strand RNA genome. Here we report that the antigen-binding (Fab) fragment of a neutralizing antibody (C5) can trigger genome release from RV-B14 to form emptied particles and neutralize virus infection. Using cryo-electron microscopy, structures of the C5 Fab in complex with the full and emptied particles have been determined at 2.3 Å and 3.0 Å resolution, respectively. Each of the 60 Fab molecules binds primarily to a region on viral protein 3 (VP3). Binding of the C5 Fabs to RV-B14 results in significant conformational changes around holes in the capsid through which the viral RNA might exit. These results are so far the highest resolution view of an antibody-virus complex and elucidate a mechanism whereby antibodies neutralize RVs and related viruses by inducing virus uncoating.
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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.