ArticleAMB Express2023
Exploring the surface epitope and nuclear localization analysis of porcine circovirus type 3 capsid protein.
Article in AMB Express, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 10 citations in OpenAlex.
- The Prevalence and Genetic Diversity of Porcine Circoviruses (PCVs) in Eastern China During 2010-2016 and 2023-2024.Veterinary sciences · 2026Article
- Immunogenicity Analysis of PCV3 Capsid Highly Expressed Using Baculovirus.International journal of molecular sciences · 2026Article
- Construction andMicrobiology spectrum · 2026Article
- Epidemiological Survey of Porcine Circovirus Types 2 and 3 in Liaoning Region of China and Preparation of Monoclonal Antibodies Against PCV3 Cap Protein.Veterinary sciences · 2026Article
- Emerging Challenges and Advances in Porcine Circovirus: A Decade in Review.Transboundary and emerging diseases · 2026Review
- Genetic Characterization and Evidence of Capsid Epitope Variation in Porcine Circovirus Type 3 Strains from Vietnamese Swine with Reproductive Disorders.Current microbiology · 2025Article
- Development of a Highly Specific Monoclonal Antibody-Based Sandwich ELISA for Rapid Detection of Porcine Circovirus Type 3.Viruses · 2025Article
- Epidemiological investigation and analysis of the infection of porcine circovirus in Xinjiang.Virology journal · 2024Article
- Identification of a conserved B-cell epitope on the capsid protein of porcine circovirus type 4.mSphere · 2024Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Porcine circovirus 3 (PCV3) is a newly emerging virus associated with porcine dermatitis and nephropathy syndrome (PDNS) and reproductive disorders, impacting global pig populations. Porcine circoviruses contain two major open reading frames (ORFs), and the ORF2 encodes the viral capsid protein (Cap). Cap is the most antigenic structural protein and an ideal candidate for the development of vaccines and diagnostic reagents. This study generated a monoclonal antibody (MAb) specific to PCV3 Cap, MAb CCC160, for diagnosis and pathogenesis studies of this novel virus. The MAb specifically recognized PCV3-infected swine lymph node tissue in an immunohistochemical analysis confirming its clinical diagnostic potential. In addition, a novel linear B-cell epitope recognized by MAb CCC160 was identified at the amino acid region 120-134 of Cap. Nuclear localization analysis of PCV3 Cap revealed a potential nuclear localization signal (NLS) in the middle region (aa 131-143) in addition to the dominant N-terminal NLS that is already known. A cell viability assay further demonstrated that the cytotoxicity of PCV3 Cap is correlated with its nuclear localization, indicating a crucial role of Cap in the pathogenic mechanism of PCV3. A full-length construct of PCV3 Cap was successfully expressed using a baculovirus expression system and purified recombinant proteins self-assembled into virus-like particles (VLPs). The protein constitution of the VLPs was confirmed by MAb CCC160 recognition, indicating the correct conformation and specificity of VLP and exhibiting the linear epitope aa 120-134 on the VLP surface. These results provide insights for developing diagnostic tools and potential VLP vaccines for PCV3, revealing its pathogenesis and antigenic properties.
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