ArticleApplied microbiology and biotechnology2020
Large-scale manufacture of VP2 VLP vaccine against porcine parvovirus in Escherichia coli with high-density fermentation.
Article in Applied microbiology and biotechnology, 2020. 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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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.
The trial behind it
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.
- Advancements in nanomaterial-based adjuvants for animal vaccines.Materials today. Bio · 2026Article
- Porcine Parvovirus virus-like particle vaccine induces long-term humoral immunity by recruiting T follicular helper and germinal center B cell responses.Frontiers in immunology · 2026Article
- Intelligence Disclosure on Deploying SpyTag/SpyCatcher for Nanoparticle Assembly.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Review
- Lipid A-modified Escherichia coli can produce porcine parvovirus virus-like particles with high immunogenicity and minimal endotoxin activity.Microbial cell factories · 2024Article
- A comprehensive approach to developing a multi-epitope vaccine againstFrontiers in immunology · 2023Article
- Article
- Self-Assembly of Porcine Parvovirus Virus-like Particles and Their Application in Serological Assay.Viruses · 2022Article
- Article
- Self-assembled raccoon dog parvovirus VP2 protein confers immunity against RDPV disease in raccoon dogs: in vitro and in vivo studies.Virology journal · 2021Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Porcine parvovirus (PPV) virus-like particles (VLPs) are a potential vaccine candidate for the prevention of parvovirus-induced reproductive failure in pregnant sows. Currently, the Escherichia coli (E. coli) expression system is the most cost-efficient to express recombinant proteins. To overcome the limitations of protein misfolding and to prepare soluble highly bioactive antigen and high yields of protein, we optimized the PPV-VP2 gene, subcloned it into pET24a, pET26b, pET28a, and pET30a, and transformed it into E. coli BL21(DE3)-Tf16 competent cells. The pET28a plasmid was selected for further manipulations because it expressed high levels of the bioactive PPV-VP2 protein. Under optimal high-density fermenting conditions in a 70-L fermenter, the total yield of wet weight E. coli cells was 124.86 g/L, and PPV-VP2 protein was 2.5 g/L. After large-scale purification with Triton X-114 two-phase extraction as well as activated carbon powder adsorption, hemagglutination (HA) titers in the purified PPV-VP2 protein reached 2
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.