ArticleVirus genes2009
Expression of porcine parvovirus VP2 gene requires codon optimized E. coli cells.
Article in Virus genes, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
7 citing papers in PubMed, 17 citations in OpenAlex.
- Isolation and complete genome analysis of Porcine Parvovirus 1 from swine with reproductive failure in southern India.Archives of microbiology · 2026Article
- Article
- Trigger factor assisted self-assembly of canine parvovirus VP2 protein into virus-like particles in Escherichia coli with high immunogenicity.Virology journal · 2018Article
- Generation of recombinant porcine parvovirus virus-like particles in Saccharomyces cerevisiae and development of virus-specific monoclonal antibodies.Journal of immunology research · 2014Article
- Article
- Phylogenetic analysis of porcine parvoviruses from swine samples in China.Virology journal · 2011Article
- Production and purification of VP2 protein of porcine parvovirus expressed in an insect-baculovirus cell system.Virology journal · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Porcine parvovirus (PPV) is a widespread infectious virus that causes serious reproductive diseases of swine and death of piglets. The gene coding for the capsid protein VP2 of PPV was amplified and inserted into the plasmid pET-32a (+), which was then used to transform Escherichia coli Rosetta, the capsid protein of PPV was fused to a polyhistidine tag, and the position of the affinity tag is in N-terminus. VP2 was expressed using different expression host bacteria, including E. coli BL21, and Rosetta, and different plasmid vectors, including pET-30a (+), pET-32a (+), and pGEX-6p-1. After selection, only the fusion protein inserted into pET-32a (+) was expressed well in E. coli Rosetta. The recombinant bacterium produced high quantities of the fusion protein VP2, about 8% in total. The expressed VP2 was antigenically similar to the native capsid protein according to a Western blot assay performed with polyclonal antibodies obtained from pigs vaccinated with PPV. A simple, easily commercialized procedure was used to purify this protein. This study provides a foundation for the application of VP2 protein in the clinical diagnosis of PPV and in the vaccination against PPV.
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