ArticleJournal of virology2020
Neutralization Mechanism of a Monoclonal Antibody Targeting a Porcine Circovirus Type 2 Cap Protein Conformational Epitope.
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 25 papers.
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Who cites it
25 citing papers in PubMed, 33 citations in OpenAlex.
- Preparation of Monoclonal Antibodies Against Porcine Circovirus Type 2 Capsid Protein and Development of a Blocking ELISA for Detection of the Antibody Against the Virus.Veterinary sciences · 2026Article
- Structural basis and immunogenic efficacy of porcine circovirus type 3 virus-like particle.Nature communications · 2026Article
- Article
- Engineered PCV2 VLPs for Antigen Delivery: A Platform for Next-Generation Veterinary Vaccines.Transboundary and emerging diseases · 2026Review
- Article
- Genetic Characterization and Evidence of Capsid Epitope Variation in Porcine Circovirus Type 3 Strains from Vietnamese Swine with Reproductive Disorders.Current microbiology · 2025Article
- Article
- Structural Capsidomics of Single-Stranded DNA Viruses.Viruses · 2025Review
- Epidemiological and genetic variation analysis of emerging porcine circovirus type 2 in Henan Province, 2023.Frontiers in veterinary science · 2025Article
- The Prevalence and Genetic Characteristics of Porcine Circovirus Type 2 in Shandong Province, China, 2018-2020.Current issues in molecular biology · 2024Article
- Identification of a conserved B-cell epitope on the capsid protein of porcine circovirus type 4.mSphere · 2024Article
- An updated phylogeography and population dynamics of porcine circovirus 2 genotypes: are they reaching an equilibrium?Frontiers in microbiology · 2024Article
- Investigation of porcine circovirus type 2 and porcine circovirus type 3 infections based on dual TaqMan fluorescent quantitative PCR method and genetic evolutionary analysis of these two viruses.Frontiers in microbiology · 2024Article
- Construction of recombinant pseudorabies virus expressing PCV2 Cap, PCV3 Cap, and IL-4: investigation of their biological characteristics and immunogenicity.Frontiers in immunology · 2024Article
- Phylogenetic Analysis and Serological Investigation of Porcine Circovirus Indicates Frequent Infection with Various Subtypes.International journal of molecular sciences · 2023Article
- Production of virus-like particles of porcine circovirus 2 in baculovirus expression system and its application for antibody detection.BMC veterinary research · 2023Article
- Identification of B-Cell Epitopes on Capsid Protein Reveals Two Potential Neutralization Mechanisms in Red-Spotted Grouper Nervous Necrosis Virus.Journal of virology · 2023Article
- Emergence of novel porcine circovirus 2d strains in Thailand, 2019-2020.Frontiers in veterinary science · 2023Article
- Immunogenicity and Immunoprotection of PCV2 Virus-like Particles Incorporating Dominant T and B Cell Antigenic Epitopes Paired with CD154 Molecules in Piglets and Mice.International journal of molecular sciences · 2022Article
- Molecular genotypic analysis of porcine circovirus type 2 reveals the predominance of PCV2d in Vietnam (2018-2020) and the association between PCV2h, the recombinant forms, and Vietnamese vaccines.Archives of virology · 2022Article
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Porcine circovirus type 2 (PCV2) is an important pathogen in swine herds, and its infection of pigs has caused severe economic losses to the pig industry worldwide. The capsid protein of PCV2 is the only structural protein that is associated with PCV2 infection and immunity. Here, we report a neutralizing monoclonal antibody (MAb), MAb 3A5, that binds to intact PCV2 virions of the PCV2a, PCV2b, and PCV2d genotypes. MAb 3A5 neutralized PCV2 by blocking viral attachment to PK15 cells. To further explore the neutralization mechanism, we resolved the structure of the PCV2 virion in complex with MAb 3A5 Fab fragments by using cryo-electron microscopy single-particle analysis. The binding sites were located at the topmost edges around 5-fold icosahedral symmetry axes, with each footprint covering amino acids from two adjacent capsid proteins. Most of the epitope residues (15/18 residues) were conserved among 2,273 PCV2 strains. Mutations of some amino acids within the epitope had significant effects on the neutralizing activity of MAb 3A5. This study reveals the molecular and structural bases of this PCV2-neutralizing antibody and provides new and important information for vaccine design and therapeutic antibody development against PCV2 infections.
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