ArticleAMB Express2020
Self-assembly into virus-like particles of the recombinant capsid protein of porcine circovirus type 3 and its application on antibodies detection.
Article in AMB Express, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 30 citations in OpenAlex.
- Establishment of an Indirect ELISA Detection Method for Porcine Circovirus 3 Based on Soluble Cap Protein.Veterinary sciences · 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
- Virus-like particle (VLP)-based indirect ELISA (iELISA) for the detection of beak and feather disease virus (BFDV) antibodies.Applied microbiology and biotechnology · 2026Article
- Development of a Highly Specific Monoclonal Antibody-Based Sandwich ELISA for Rapid Detection of Porcine Circovirus Type 3.Viruses · 2025Article
- Detection of Porcine Circovirus Type 3 in Free-Ranging Wild Boars and Ticks in Jiangsu Province, China.Viruses · 2025Article
- The porcine circovirus 3 humoral response: characterization of maternally derived antibodies and dynamic following experimental infection.Microbiology spectrum · 2024Article
- Identification of a conserved B-cell epitope on the capsid protein of porcine circovirus type 4.mSphere · 2024Article
- Recombinantly expressed virus-like particles (VLPs) of canine circovirus for development of an indirect ELISA.Veterinary research communications · 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
- Recombinant Orf virus induced antibody production against capsid protein of porcine circovirus type 3 in mice.Veterinary research communications · 2023Article
- Immunogenicity Analysis of PCV3 Recombinant Capsid Protein Virus-like Particles and Their Application in Antibodies Detection.International journal of molecular sciences · 2023Article
- Platforms, advances, and technical challenges in virus-like particles-based vaccines.Frontiers in immunology · 2023Review
- Porcine Circovirus Type 3: Diagnostics, Genotyping, and Challenges in Vaccine Development.Transboundary and emerging diseases · 2023Review
- Self-Assembly of Porcine Parvovirus Virus-like Particles and Their Application in Serological Assay.Viruses · 2022Article
- Virus-like Particles: Fundamentals and Biomedical Applications.International journal of molecular sciences · 2022Review
- Article
- Pathogenic Characterization of a Porcine Circovirus Type 3 Isolate from Heilongjiang, China.Disease markers · 2021Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
PCV3 capsid protein (Cap) is an important antigen for diagnosis and vaccine development. To achieve high-level expression of recombinant PCV3 Cap in Escherichia coli (E. coli), the gene of wild-type entire Cap (wt-eCap) was amplified from clinical samples, and three optimized entire Cap (opti-eCap) and one optimized Cap deleted nuclear location signal (NLS) (opti-dCap) gene fragments encoding the same amino acid sequence with wt-eCap were synthesized based on the codon bias of E. coli. Those gene fragments were inserted into the pET30a expression vector. One recombinant strain with the highest expressed soluble eCap from four entire Cap (one wt-eCap and three opti-eCap) and one recombinant strain expressed opti-dCap were selected for further purification. The purified eCap and dCap were identified by transmission electron microscopy (TEM), a large number of round hollow particles with a diameter of 10 nm virus-like particles (VLPs) were observed in eCap, whereas irregular aggregation of proteins observed in dCap. After formation the VLPs were applied as a coating antigen to establish an indirect ELISA (I-ELISA) for detection of PCV3-specific antibody in swine serum. 373 clinical swine serum samples from China collected in 2019 were tested utilizing the VLP-based I-ELISA method under optimized conditions. To the best of our knowledge, this is the first report of self-assembly into VLPs of PCV3 recombinant Cap. Our results demonstrated that the VLP-based I-ELISA will be a valuable tool for detecting the presence of PCV3 antibodies in serum samples and will facilitate screening of large numbers of swine serum for clinical purposes.
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