ArticleJournal of virology2013
Structural and functional analysis of coxsackievirus A9 integrin αvβ6 binding and uncoating.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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.
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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
34 citing papers in PubMed, 52 citations in OpenAlex.
- The multifaceted roles of fibronectin in viral pathogenesis.Archives of virology · 2026Review
- Establishment of a Panel of Human Cell Lines to Identify Cellular Receptors Used byInternational journal of molecular sciences · 2025Article
- Protease-Independent Production of Poliovirus Virus-like Particles in Pichia pastoris: Implications for Efficient Vaccine Development and Insights into Capsid Assembly.Microbiology spectrum · 2023Article
- Review
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- Structural Studies Reveal that Endosomal Cations Promote Formation of Infectious Coxsackievirus A9 A-Particles, Facilitating RNA and VP4 Release.Journal of virology · 2022Article
- 2'-Fucosyllactose Inhibits Coxsackievirus Class A Type 9 Infection by Blocking Virus Attachment and Internalisation.International journal of molecular sciences · 2022Article
- The RGD-binding integrins αvβ6 and αvβ8 are receptors for mouse adenovirus-1 and -3 infection.PLoS pathogens · 2021Article
- Tradeoffs for a viral mutant with enhanced replication speed.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Antivirals blocking entry of enteroviruses and therapeutic potential.Journal of biomedical science · 2021Review
- Structure of Nora virus at 2.7 Å resolution and implications for receptor binding, capsid stability and taxonomy.Scientific reports · 2020Article
- Structures of Echovirus 30 in complex with its receptors inform a rational prediction for enterovirus receptor usage.Nature communications · 2020Article
- Article
- Recombination Events and Conserved Nature of Receptor Binding Motifs in Coxsackievirus A9 Isolates.Viruses · 2020Article
- Article
- Evolutionary and Structural Overview of Human Picornavirus Capsid Antibody Evasion.Frontiers in cellular and infection microbiology · 2019Review
- Image processing for cryogenic transmission electron microscopy of symmetry-mismatched complexes.Bioscience reports · 2018Article
- Intrinsically-disordered N-termini in human parechovirus 1 capsid proteins bind encapsidated RNA.Scientific reports · 2018Article
- Unraveling the Motions behind Enterovirus 71 Uncoating.Biophysical journal · 2018Article
- Rules of engagement between αvβ6 integrin and foot-and-mouth disease virus.Nature communications · 2017Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coxsackievirus A9 (CVA9) is an important pathogen of the Picornaviridae family. It utilizes cellular receptors from the integrin αv family for binding to its host cells prior to entry and genome release. Among the integrins tested, it has the highest affinity for αvβ6, which recognizes the arginine-glycine-aspartic acid (RGD) loop present on the C terminus of viral capsid protein, VP1. As the atomic model of CVA9 lacks the RGD loop, we used surface plasmon resonance, electron cryo-microscopy, and image reconstruction to characterize the capsid-integrin interactions and the conformational changes on genome release. We show that the integrin binds to the capsid with nanomolar affinity and that the binding of integrin to the virion does not induce uncoating, thereby implying that further steps are required for release of the genome. Electron cryo-tomography and single-particle image reconstruction revealed variation in the number and conformation of the integrins bound to the capsid, with the integrin footprint mapping close to the predicted site for the exposed RGD loop on VP1. Comparison of empty and RNA-filled capsid reconstructions showed that the capsid undergoes conformational changes when the genome is released, so that the RNA-capsid interactions in the N termini of VP1 and VP4 are lost, VP4 is removed, and the capsid becomes more porous, as has been reported for poliovirus 1, human rhinovirus 2, enterovirus 71, and coxsackievirus A7. These results are important for understanding the structural basis of integrin binding to CVA9 and the molecular events leading to CVA9 cell entry and uncoating.
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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.