ArticlePLoS pathogens2012
Insights into minor group rhinovirus uncoating: the X-ray structure of the HRV2 empty capsid.
Article in PLoS pathogens, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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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
72 citing papers in PubMed, 106 citations in OpenAlex.
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- Antigenic characterization and mapping of a conserved neutralizing epitope on VP1 of coxsackievirus A5.Frontiers in immunology · 2026Article
- Cryo-EM structure of the Seneca Valley virus A-particle and related structural states.Journal of virology · 2025Article
- DMSO might impact ligand binding, capsid stability, and RNA interaction in viral preparations.Scientific reports · 2024Article
- Cryo-EM of human rhinovirus reveals capsid-RNA duplex interactions that provide insights into virus assembly and genome uncoating.Communications biology · 2024Article
- Endosome rupture enables enteroviruses from the family Picornaviridae to infect cells.Communications biology · 2024Article
- X-Ray Crystallography of Viruses.Sub-cellular biochemistry · 2024Review
- Stabilization of the Quadruplex-Forming G-Rich Sequences in the Rhinovirus Genome Inhibits Uncoating-Role of NaViruses · 2023Article
- Article
- Molecular Determinants of Human Rhinovirus Infection, Assembly, and Conformational Stability at Capsid Protein Interfaces.Journal of virology · 2022Article
- Structural Insights into Common and Host-Specific Receptor-Binding Mechanisms in Algal Picorna-like Viruses.Viruses · 2022Article
- Structure of Human Enterovirus 70 and Its Inhibition by Capsid-Binding Compounds.Journal of virology · 2022Article
- Membrane Interactions and Uncoating of Aichi Virus, a Picornavirus That Lacks a VP4.Journal of virology · 2022Article
- Cryo-EM Structure of a Possum Enterovirus.Viruses · 2022Article
- Review
- ICAM-1 induced rearrangements of capsid and genome prime rhinovirus 14 for activation and uncoating.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Virion structure andJournal of virology · 2021Article
- Rhinovirus and Cell Death.Viruses · 2021Review
- Antivirals blocking entry of enteroviruses and therapeutic potential.Journal of biomedical science · 2021Review
- Capsid opening enables genome release of iflaviruses.Science advances · 2021Article
12 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Upon attachment to their respective receptor, human rhinoviruses (HRVs) are internalized into the host cell via different pathways but undergo similar structural changes. This ultimately results in the delivery of the viral RNA into the cytoplasm for replication. To improve our understanding of the conformational modifications associated with the release of the viral genome, we have determined the X-ray structure at 3.0 Å resolution of the end-stage of HRV2 uncoating, the empty capsid. The structure shows important conformational changes in the capsid protomer. In particular, a hinge movement around the hydrophobic pocket of VP1 allows a coordinated shift of VP2 and VP3. This overall displacement forces a reorganization of the inter-protomer interfaces, resulting in a particle expansion and in the opening of new channels in the capsid core. These new breaches in the capsid, opening one at the base of the canyon and the second at the particle two-fold axes, might act as gates for the externalization of the VP1 N-terminus and the extrusion of the viral RNA, respectively. The structural comparison between native and empty HRV2 particles unveils a number of pH-sensitive amino acid residues, conserved in rhinoviruses, which participate in the structural rearrangements involved in the uncoating process.
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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.