ArticleJournal of virology2020
Cryo-electron Microscopy Structure, Assembly, and Mechanics Show Morphogenesis and Evolution of Human Picobirnavirus.
Article in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 24 citations in OpenAlex.
- Viruses under mechanical force: Implications and applications.Virus research · 2026Review
- Calicivirus assembly and stability are mediated by the N-terminal domain of the capsid protein with the involvement of the viral genome.PLoS pathogens · 2025Article
- Comparative analysis of the extent of protein-protein interactions in icosahedral viral capsids.Protein science : a publication of the Protein Society · 2025Article
- "Paraxenoviridae", a putative family of ubiquitous marine bacteriophages with double-stranded RNA genomes.bioRxiv : the preprint server for biology · 2025Article
- Structure of the T=13 capsid of infectious pancreatic necrosis virus (IPNV)-a salmonid birnavirus.Journal of virology · 2025Article
- "Paraxenoviridae", a putative family of globally distributed marine bacteriophages with double-stranded RNA genomes.The ISME journal · 2025Article
- High-resolution comparative atomic structures of two Giardiavirus prototypes infecting G. duodenalis parasite.PLoS pathogens · 2024Article
- Mechanical Properties of Viruses.Sub-cellular biochemistry · 2024Review
- Capsid structure of a fungal dsRNA megabirnavirus reveals its previously unidentified surface architecture.PLoS pathogens · 2023Article
- The structure of a plant-specific partitivirus capsid reveals a unique coat protein domain architecture with an intrinsically disordered protrusion.Communications biology · 2021Article
- Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Despite their diversity, most double-stranded-RNA (dsRNA) viruses share a specialized T=1 capsid built from dimers of a single protein that provides a platform for genome transcription and replication. This ubiquitous capsid remains structurally undisturbed throughout the viral cycle, isolating the genome to avoid triggering host defense mechanisms. Human picobirnavirus (hPBV) is a dsRNA virus frequently associated with gastroenteritis, although its pathogenicity is yet undefined. Here, we report the cryo-electron microscopy (cryo-EM) structure of hPBV at 2.6-Å resolution. The capsid protein (CP) is arranged in a single-shelled, ∼380-Å-diameter T=1 capsid with a rough outer surface similar to that of dsRNA mycoviruses. The hPBV capsid is built of 60 quasisymmetric CP dimers (A and B) stabilized by domain swapping, and only the CP-A N-terminal basic region interacts with the packaged nucleic acids. hPBV CP has an α-helical domain with a fold similar to that of fungal partitivirus CP, with many domain insertions in its C-terminal half. In contrast to dsRNA mycoviruses, hPBV has an extracellular life cycle phase like complex reoviruses, which indicates that its own CP probably participates in cell entry. Using an
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