ArticleBioscience reports2020
Structural insight into the type-specific epitope of porcine circovirus type 3.
Article in Bioscience reports, 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 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
11 citing papers in PubMed.
- Establishment of an Indirect ELISA Detection Method for Porcine Circovirus 3 Based on Soluble Cap Protein.Veterinary sciences · 2026Article
- Immunogenicity Analysis of PCV3 Capsid Highly Expressed Using Baculovirus.International journal of molecular sciences · 2026Article
- Emerging Challenges and Advances in Porcine Circovirus: A Decade in Review.Transboundary and emerging diseases · 2026Review
- Epidemiological investigation and analysis of the infection of porcine circovirus in Xinjiang.Virology journal · 2024Article
- Preparation of Monoclonal Antibodies against the Capsid Protein and Development of an Epitope-Blocking Enzyme-Linked Immunosorbent Assay for Detection of the Antibody against Porcine Circovirus 3.Animals : an open access journal from MDPI · 2024Article
- Revisiting Porcine Circovirus Infection: Recent Insights and Its Significance in the Piggery Sector.Vaccines · 2023Review
- Porcine Circovirus Type 3: Diagnostics, Genotyping, and Challenges in Vaccine Development.Transboundary and emerging diseases · 2023Review
- Review
- High Prevalence of Porcine Circovirus 3 in Hungarian Pig Herds: Results of a Systematic Sampling Protocol.Viruses · 2022Article
- Colorimetric Kit for Rapid Porcine Circovirus 2 (PCV-2) Diagnosis.Pathogens (Basel, Switzerland) · 2022Article
- Review
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The recently identified pathogenic Porcine circovirus type 3 (PCV3) may threaten to reduce the pig population dramatically worldwide. In our previous study, a PCV3-specific monoclonal antibody (mAb-1H11) was successfully applied in immune-histochemistry staining and ELISA, which specifically recognize PCV3 capsid protein in PCV3-positive pig tissues. In the present study, we expressed and purified the soluble sole capsid protein of PCV3. The purified capsid protein was capable of self-assembly into virus-like-particles (VLPs), which is validated by transmission electron microscopy and dynamic light scattering assays. Moreover, the epitope of mAb-1H11 was identified in the CD-loop region (a.a. 72-79) on the VLP surface, which is confirmed by PCV2-PCV3 epitope swapping assay. For the first time, we determined the cryo-EM structure of PCV3-VLP at 8.5 Å resolution that reveals the detailed structural information of PCV3-VLP. In our cryo-EM structure, PCV3-VLP is composed of 60 capsid protein subunits assembled with T = 1 icosahedral symmetry. Consistent to our bio-dot Western blot assay, the structural comparison between PCV3 and PCV2 revealed significant structural differences in the surface-exposed loops, including the CD-loop (a.a. 72-79) and the EF-loop (a.a. 109-131). Our work provides a structural framework for engineering future PCV3 vaccine and diagnosis kits development.
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