ArticleJournal of virology2012
Recognition of the different structural forms of the capsid protein determines the outcome following infection with porcine circovirus type 2.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 55 citations in OpenAlex.
- A multi species autophagy-inducing nano-vaccine platform: uncovering immunoenhancement properties of PCV2 cap nanoparticles.Journal of nanobiotechnology · 2026Article
- Engineered PCV2 VLPs for Antigen Delivery: A Platform for Next-Generation Veterinary Vaccines.Transboundary and emerging diseases · 2026Review
- PCV2 Cap protein nuclear import via importin α/β receptor: molecular insights and antiviral potential.Frontiers in microbiology · 2025Article
- Generation of porcine circovirus type 4 virus-like particles and their use to detect serum antibodies.Archives of virology · 2024Article
- Exploring the surface epitope and nuclear localization analysis of porcine circovirus type 3 capsid protein.AMB Express · 2023Article
- Research Progress on the Development of Porcine Reproductive and Respiratory Syndrome Vaccines.Veterinary sciences · 2023Review
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- Porcine Circovirus 2 Manipulates the PERK-ERO1α Axis of the Endoplasmic Reticulum To Favor Its Replication by Derepressing Viral DNA from HMGB1 Sequestration within Nuclei.Journal of virology · 2021Article
- Nucleolar protein NPM1 is essential for circovirus replication by binding to viral capsid.Virulence · 2020Article
- Targeted Alteration of Antibody-Based Immunodominance Enhances the Heterosubtypic Immunity of an Experimental PCV2 Vaccine.Vaccines · 2020Article
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- PCV2 Induces Reactive Oxygen Species To Promote Nucleocytoplasmic Translocation of the Viral DNA Binding Protein HMGB1 To Enhance Its Replication.Journal of virology · 2020Article
- Neutralization Mechanism of a Monoclonal Antibody Targeting a Porcine Circovirus Type 2 Cap Protein Conformational Epitope.Journal of virology · 2020Article
- The Carboxyl Terminus of the Porcine Circovirus Type 2 Capsid Protein Is Critical to Virus-Like Particle Assembly, Cell Entry, and Propagation.Journal of virology · 2020Article
- Immunogenicity of plant-produced porcine circovirus-like particles in mice.Plant biotechnology journal · 2019Article
- Phylogeographic and genetic characterization of porcine circovirus type 2 in Taiwan from 2001-2017.Scientific reports · 2019Article
- Changes on the viral capsid surface during the evolution of porcine circovirus type 2 (PCV2) from 2009 till 2018 may lead to a better receptor binding.Virus evolution · 2019Article
- The level of decoy epitope in PCV2 vaccine affects the neutralizing activity of sera in the immunized animals.Biochemical and biophysical research communications · 2018Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Porcine circovirus type 2 (PCV2) capsid protein (CP) is the only protein necessary for the formation of the virion capsid, and recombinant CP spontaneously forms virus-like particles (VLPs). Located within a single CP subunit is an immunodominant epitope consisting of residues 169 to 180 [CP(169-180)], which is exposed on the surface of the subunit, but, in the structural context of the VLP, the epitope is buried and inaccessible to antibody. High levels of anti-CP(169-180) activity are associated with porcine circovirus-associated disease (PCVAD). The purpose of this study was to investigate the role of the immune response to monomer CP in the development of PCVAD. The approach was to immunize pigs with CP monomer, followed by challenge with PCV2 and porcine reproductive and respiratory syndrome virus (PRRSV). To maintain the CP immunogen as a stable monomer, CP(43-233) was fused to ubiquitin (Ub-CP). Size exclusion chromatography showed that Ub-CP was present as a single 33-kDa protein. Pigs immunized with Ub-CP developed a strong antibody response to PCV2, including antibodies against CP(169-180). However, only low levels of virus neutralizing activity were detected, and viremia levels were similar to those of nonimmunized pigs. As a positive control, immunization with baculovirus-expressed CP (Bac-CP) resulted in high levels of virus neutralizing activity, small amounts of anti-CP(169-180) activity, and the absence of viremia in pigs following virus challenge. The data support the role of CP(169-180) as an immunological decoy and illustrate the importance of the structural form of the CP immunogen in determining the outcome following infection.
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