ArticleJournal of virology2011
The 2.3-angstrom structure of porcine circovirus 2.
Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 92 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.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
92 citing papers in PubMed, 199 citations in OpenAlex.
- Structural basis and immunogenic efficacy of porcine circovirus type 3 virus-like particle.Nature communications · 2026Article
- Preparation and Immune Protective Efficacy Evaluation of PCV2d Cap-COS Bioconjugate Candidate Vaccine.ACS omega · 2026Article
- Engineered PCV2 VLPs for Antigen Delivery: A Platform for Next-Generation Veterinary Vaccines.Transboundary and emerging diseases · 2026Review
- Article
- Identification and biochemical characterization of a novel porcine circovirus associated with porcine respiratory and diarrheal diseases.Microbiology spectrum · 2025Article
- Engineering a bivalent nanoparticle vaccine with PCV2 capsid protein and PRRSV epitopes.Journal of nanobiotechnology · 2025Article
- Structural Capsidomics of Single-Stranded DNA Viruses.Viruses · 2025Review
- Aquatic circoviruses: emerging pathogens in global aquaculture - from discovery to disease management.Journal of virology · 2025Review
- Expression of recombinant Cap antigen of porcine circovirus type 2 in the chloroplast ofFrontiers in plant science · 2025Article
- The Decade of Porcine Circovirus Type 2 (PCV2) in Thailand: Phylodynamic and Molecular Epidemiology.Transboundary and emerging diseases · 2025Article
- Review
- Explicit description of viral capsid subunit shapes by unfolding dihedrons.Communications biology · 2024Article
- 2024 taxonomy update for the family Circoviridae.Archives of virology · 2024Review
- Identification of a conserved B-cell epitope on the capsid protein of porcine circovirus type 4.mSphere · 2024Article
- The Structure ofViruses · 2024Article
- Insights into the inhibition of protospacer integration via direct interaction between Cas2 and AcrVA5.Nature communications · 2024Article
- Recombinantly expressed virus-like particles (VLPs) of canine circovirus for development of an indirect ELISA.Veterinary research communications · 2024Article
- Identification of the Effects of 5-Azacytidine on Porcine Circovirus Type 2 Replication in Porcine Kidney Cells.Veterinary sciences · 2024Article
- Article
- From obscurity to urgency: a comprehensive analysis of the rising threat of duck circovirus.Veterinary research · 2024Review
32 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Porcine circovirus 2 (PCV2) is a T=1 nonenveloped icosahedral virus that has had severe impact on the swine industry. Here we report the crystal structure of an N-terminally truncated PCV2 virus-like particle at 2.3-Å resolution, and the cryo-electron microscopy (cryo-EM) image reconstruction of a full-length PCV2 virus-like particle at 9.6-Å resolution. This is the first atomic structure of a circovirus. The crystal structure revealed that the capsid protein fold is a canonical viral jelly roll. The loops connecting the strands of the jelly roll define the limited features of the surface. Sulfate ions interacting with the surface and electrostatic potential calculations strongly suggest a heparan sulfate binding site that allows PCV2 to gain entry into the cell. The crystal structure also allowed previously determined epitopes of the capsid to be visualized. The cryo-EM image reconstruction showed that the location of the N terminus, absent in the crystal structure, is inside the capsid. As the N terminus was previously shown to be antigenic, it may externalize through viral "breathing."
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What OpenQuestion holds
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.