ArticleNature communications2023
A human monoclonal antibody binds within the poliovirus receptor-binding site to neutralize all three serotypes.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 14 citations in OpenAlex.
- Cross-Neutralizing and Broadly Neutralizing Human Antibodies Against Nonenveloped Viruses.European journal of immunology · 2026Review
- A Panel of VHH Antibodies Against Sabin Type 1 Poliovirus D-Antigen Reveals Strain-Specific and Cross-Serotype Reactivity.Viruses · 2026Article
- Progress in enterovirus D68-neutralizing antibodies and vaccines.Journal of virology · 2026Review
- VP1 molecular evolution of type 2 immunodeficiency-related vaccine-derived polioviruses (iVDPV2) in a patient with primary immunodeficiency disease (PID).Virus genes · 2026Article
- Structural insight into the assembly and D antigenicity of polio type 1 stabilized virus-like particles.NPJ vaccines · 2026Article
- Neutralizing human monoclonal antibodies to poliovirus map to the receptor binding site.Nature communications · 2026Article
- A review of post-exposure strategies for high-consequence viral pathogens in the laboratory.Clinical microbiology reviews · 2025Review
- Viro3D: a comprehensive database of virus protein structure predictions.Molecular systems biology · 2025Article
- Article
- Advances and challenges in poliomyelitis vaccines: a comprehensive review of development, production, and global deployment.Frontiers in public health · 2025Review
- Non-lytic spread of poliovirus requires the nonstructural protein 3CD.bioRxiv : the preprint server for biology · 2024Article
- Vaccine Potency and Structure of Yeast-Produced Polio Type 2 Stabilized Virus-like Particles.Vaccines · 2024Article
- Enterovirus virus-like-particle and inactivated poliovirus vaccines do not elicit substantive cross-reactive antibody responses.PLoS pathogens · 2024Article
Corrections and comments
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Authors and funding
15 authors at 3 institutions in 1 country.
Funding
Abstract
Global eradication of poliovirus remains elusive, and it is critical to develop next generation vaccines and antivirals. In support of this goal, we map the epitope of human monoclonal antibody 9H2 which is able to neutralize the three serotypes of poliovirus. Using cryo-EM we solve the near-atomic structures of 9H2 fragments (Fab) bound to capsids of poliovirus serotypes 1, 2, and 3. The Fab-virus complexes show that Fab interacts with the same binding mode for each serotype and at the same angle of interaction relative to the capsid surface. For each of the Fab-virus complexes, we find that the binding site overlaps with the poliovirus receptor (PVR) binding site and maps across and into a depression in the capsid called the canyon. No conformational changes to the capsid are induced by Fab binding for any complex. Competition binding experiments between 9H2 and PVR reveal that 9H2 impedes receptor binding. Thus, 9H2 outcompetes the receptor to neutralize poliovirus. The ability to neutralize all three serotypes, coupled with the critical importance of the conserved receptor binding site make 9H2 an attractive antiviral candidate for future development.
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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.