ArticleVirology journal2010
Production and purification of VP2 protein of porcine parvovirus expressed in an insect-baculovirus cell system.
Article in Virology journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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
10 citing papers in PubMed, 22 citations in OpenAlex.
- Isolation and complete genome analysis of Porcine Parvovirus 1 from swine with reproductive failure in southern India.Archives of microbiology · 2026Article
- Donor Plasmid Optimization Enhances Expression of Feline Parvovirus VP2 Protein in the Baculovirus Expression Vector System.Vaccines · 2026Article
- Article
- Article
- Investigation of Kluyveromyces marxianus as a novel host for large-scale production of porcine parvovirus virus-like particles.Microbial cell factories · 2021Article
- Large-scale manufacture of VP2 VLP vaccine against porcine parvovirus in Escherichia coli with high-density fermentation.Applied microbiology and biotechnology · 2020Article
- Nanobody‑horseradish peroxidase and -EGFP fusions as reagents to detect porcine parvovirus in the immunoassays.Journal of nanobiotechnology · 2020Article
- Article
- Influence of minor displacements in loops of the porcine parvovirus VP2 capsid on virus-like particles assembly and the induction of antibody responses.Virus genes · 2013Article
- A novel recombinant pseudorabies virus expressing parvovirus VP2 gene: Immunogenicity and protective efficacy in swine.Virology journal · 2011Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The porcine parvovirus (PPV) VP2 protein was expressed in an insect-baculovirus cell system and was purified using Ni-NTA affinity column chromatography. The recombinant 6-His-tagged VP2 protein with molecular mass (Mr) of about 64 kDa was detected by anti-his antibody and anti-PPV serum. Electron microscopy showed that the purified VP2 protein assembled into spherical particles with diameters ranging from 20 to 22 nm. The expressed VP2 was antigenically similar to the native capsid protein according to HA and a Western blotting assay performed with polyclonal antibodies collected from an outbreak of PPV in one farm. This study provides a foundation for the application of VP2 protein in the clinical diagnosis of PPV or in the vaccination against PPV in the future.
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Registered trials
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