ArticleCommunications biology2022
Cryo-electron microscopy and image classification reveal the existence and structure of the coxsackievirus A6 virion.
Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.
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
17 citing papers in PubMed, 1 synthesis or guideline pooled it, 15 citations in OpenAlex.
- Recent advances on coxsackievirus A6 vaccine research.Frontiers in immunology · 2025Pooled it
- Particles of echovirus 18 open to release their genomes in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Open questions in enterovirus uncoating.Journal of virology · 2026Review
- A single residue in the VP3 capsid protein governs virulence and informs live-attenuated vaccine design for coxsackievirus A6.Journal of virology · 2026Article
- A conserved VP1-286 epitope governs neutralization and immune escape in Coxsackievirus A6.Frontiers in immunology · 2026Article
- Serial passagingFrontiers in cellular and infection microbiology · 2026Article
- Molecular mechanisms of receptor recognition and antibody neutralization of coxsackievirus A6.Nature communications · 2025Article
- Cryo-EM structure of the Seneca Valley virus A-particle and related structural states.Journal of virology · 2025Article
- Comparative analysis of the extent of protein-protein interactions in icosahedral viral capsids.Protein science : a publication of the Protein Society · 2025Article
- A single amino acid mutation in VP1 of coxsackievirus A6 determining efficiency of VP0 cleavage and proliferation.Journal of virology · 2025Article
- Enterovirus-like particles encapsidate RNA and exhibit decreased stability due to lack of maturation.PLoS pathogens · 2025Article
- Optimization of Enterovirus-like Particle Production and Purification Using Design of Experiments.Pathogens (Basel, Switzerland) · 2025Article
- Endosome rupture enables enteroviruses from the family Picornaviridae to infect cells.Communications biology · 2024Article
- Emergence of Recombinant Subclade D3/Y in Coxsackievirus A6 Strains in Hand-Foot-and-Mouth Disease (HFMD) Outbreak in India, 2022.Microorganisms · 2024Article
- Uncovering Structural Plasticity ofResearch square · 2024Article
- 'Tomato flu' a new epidemic in India: Virology, epidemiology, and clinical features.New microbes and new infections · 2023Review
- Coxsackievirus A6 was the most common enterovirus serotype causing hand, foot, and mouth disease in Shiyan City, central China.World journal of clinical cases · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coxsackievirus A6 (CV-A6) has recently overtaken enterovirus A71 and CV-A16 as the primary causative agent of hand, foot, and mouth disease worldwide. Virions of CV-A6 were not identified in previous structural studies, and it was speculated that the virus is unique among enteroviruses in using altered particles with expanded capsids to infect cells. In contrast, the virions of other enteroviruses are required for infection. Here we used cryo-electron microscopy (cryo-EM) to determine the structures of the CV-A6 virion, altered particle, and empty capsid. We show that the CV-A6 virion has features characteristic of virions of other enteroviruses, including a compact capsid, VP4 attached to the inner capsid surface, and fatty acid-like molecules occupying the hydrophobic pockets in VP1 subunits. Furthermore, we found that in a purified sample of CV-A6, the ratio of infectious units to virions is 1 to 500. Therefore, it is likely that virions of CV-A6 initiate infection, like those of other enteroviruses. Our results provide evidence that future vaccines against CV-A6 should target its virions instead of the antigenically distinct altered particles. Furthermore, the structure of the virion provides the basis for the rational development of capsid-binding inhibitors that block the genome release of CV-A6.
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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.