ArticleNature microbiology2019
Atomic structures of enterovirus D68 in complex with two monoclonal antibodies define distinct mechanisms of viral neutralization.
Article in Nature microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed.
- Seroepidemiology of Enterovirus D68 in Xiamen Children: A Cross-Sectional Study in 2022.Viruses · 2026Article
- A dual-receptor checkpoint primes enterovirus D68 for respiratory cell entry.Nature communications · 2026Article
- An RNA-to-RNA pipeline for rapid antiviral antibody development.Molecular therapy : the journal of the American Society of Gene Therapy · 2026Article
- Progress in enterovirus D68-neutralizing antibodies and vaccines.Journal of virology · 2026Review
- Comparative immunogenic and structural analysis of virus-like particle and inactivated whole-virion vaccines against enterovirus D68.Molecular therapy. Nucleic acids · 2026Article
- Decoding the complex receptor landscape of enterovirus D68.PLoS pathogens · 2026Review
- Epidemiological and Clinical Characteristics of the Enterovirus D68 Outbreak in Spain in 2024.Journal of medical virology · 2026Article
- Enterovirus D68 receptor usage: from static attachment to dynamic entry.Journal of virology · 2026Review
- Respiratory enterovirus D68: virology, clinical surveillance, host-pathogen interactions, and therapeutic prospects.Frontiers in cellular and infection microbiology · 2026Review
- Identification of key amino acids defining conformational neutralizing epitopes of coxsackievirus A5 using monoclonal antibody escape mutants.Frontiers in immunology · 2026Article
- Review
- Structural insights from vaccine candidates for EV-D68.Communications biology · 2025Article
- MFSD6 is an entry receptor for enterovirus D68.Nature · 2025Article
- Article
- Computational discovery of natural inhibitors targeting enterovirus D68 3C protease using molecular docking pharmacokinetics and dynamics simulations.Scientific reports · 2025Article
- A single residue switch mediates the broad neutralization of Rotaviruses.Nature communications · 2025Article
- Emerging Therapeutics in the Fight Against EV-D68: A Review of Current Strategies.Influenza and other respiratory viruses · 2024Review
- A self-amplifying RNA vaccine prevents enterovirus D68 infection and disease in preclinical models.Science translational medicine · 2024Article
- Enterovirus virus-like-particle and inactivated poliovirus vaccines do not elicit substantive cross-reactive antibody responses.PLoS pathogens · 2024Article
- Neutralizing antibody landscape of the non-polio Enteroviruses and future strategy.Frontiers in immunology · 2024Review
Corrections and comments
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Authors and funding
24 authors.
Funding
Abstract
Enterovirus D68 (EV-D68) undergoes structural transformation between mature, cell-entry intermediate (A-particle) and empty forms throughout its life cycle. Structural information for the various forms and antibody-bound capsids will facilitate the development of effective vaccines and therapeutics against EV-D68 infection, which causes childhood respiratory and paralytic diseases worldwide. Here, we report the structures of three EV-D68 capsid states representing the virus at major phases. We further describe two original monoclonal antibodies (15C5 and 11G1) with distinct structurally defined mechanisms for virus neutralization. 15C5 and 11G1 engage the capsid loci at icosahedral three-fold and five-fold axes, respectively. To block viral attachment, 15C5 binds three forms of capsids, and triggers mature virions to transform into A-particles, mimicking engagement by the functional receptor ICAM-5, whereas 11G1 exclusively recognizes the A-particle. Our data provide a structural and molecular explanation for the transition of picornavirus capsid conformations and demonstrate distinct mechanisms for antibody-mediated neutralization.
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