ArticleScience advances2018
Discovery and structural characterization of a therapeutic antibody against coxsackievirus A10.
Article in Science advances, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 26 citations in OpenAlex.
- Antigenic characterization and mapping of a conserved neutralizing epitope on VP1 of coxsackievirus A5.Frontiers in immunology · 2026Article
- Identification of key amino acids defining conformational neutralizing epitopes of coxsackievirus A5 using monoclonal antibody escape mutants.Frontiers in immunology · 2026Article
- Article
- Discovery of a broad-spectrum monoclonal antibody recognizing a conserved, linear epitope WFYDGYPT on VP1 protein of Enterovirus A species.Virology journal · 2024Article
- Broadly therapeutic antibody provides cross-serotype protection against enteroviruses via Fc effector functions and by mimicking SCARB2.Nature microbiology · 2024Article
- Neutralizing antibody landscape of the non-polio Enteroviruses and future strategy.Frontiers in immunology · 2024Review
- Article
- VP2 residue N142 of coxsackievirus A10 is critical for the interaction with KREMEN1 receptor and neutralizing antibodies and the pathogenicity in mice.PLoS pathogens · 2023Article
- In silico epitope prediction and evolutionary analysis reveals capsid mutation patterns for enterovirus B.PloS one · 2023Article
- High-resolution structural analysis of enterovirus-reactive polyclonal antibodies in complex with whole virions.PNAS nexus · 2022Article
- Cryo-electron microscopy and image classification reveal the existence and structure of the coxsackievirus A6 virion.Communications biology · 2022Article
- Bioinformatics-based prediction of conformational epitopes for Enterovirus A71 and Coxsackievirus A16.Scientific reports · 2021Article
- Cryo-EM structures reveal the molecular basis of receptor-initiated coxsackievirus uncoating.Cell host & microbe · 2021Article
- Serotype specific epitopes identified by neutralizing antibodies underpin immunogenic differences in Enterovirus B.Nature communications · 2020Article
- Molecular basis of Coxsackievirus A10 entry using the two-in-one attachment and uncoating receptor KRM1.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Identification of Antibodies with Non-overlapping Neutralization Sites that Target Coxsackievirus A16.Cell host & microbe · 2020Article
- Cryo-EM Studies of Virus-Antibody Immune Complexes.Virologica Sinica · 2020Review
- Hand-foot-and-mouth disease virus receptor KREMEN1 binds the canyon of Coxsackie Virus A10.Nature communications · 2020Article
- Advances in Antigenic Peptide-Based Vaccine and Neutralizing Antibodies against Viruses Causing Hand, Foot, and Mouth Disease.International journal of molecular sciences · 2019Review
Corrections and comments
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Authors and funding
21 authors at 3 institutions in 2 countries.
Funding
Abstract
Coxsackievirus A10 (CVA10) recently emerged as a major pathogen of hand, foot, and mouth disease and herpangina in children worldwide, and lack of a vaccine or a cure against CVA10 infections has made therapeutic antibody identification a public health priority. By targeting a local isolate, CVA10-FJ-01, we obtained a potent antibody, 2G8, against all three capsid forms of CVA10. We show that 2G8 exhibited both 100% preventive and 100% therapeutic efficacy against CVA10 infection in mice. Comparisons of the near-atomic cryo-electron microscopy structures of the three forms of CVA10 capsid and their complexes with 2G8 Fab reveal that a single Fab binds a border region across the three capsid proteins (VP1 to VP3) and explain 2G8's remarkable cross-reactivities against all three capsid forms. The atomic structures of this first neutralizing antibody of CVA10 should inform strategies for designing vaccines and therapeutics against CVA10 infections.
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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.