ArticleBiotechnology letters2020
A classical swine fever virus E2 fusion protein produced in plants elicits a neutralizing humoral immune response in mice and pigs.
Article in Biotechnology letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Plant-derived vaccines for veterinary disease management in ruminants and swine.Biotechnology letters · 2026Review
- Review
- Advances in Subcellular Accumulation Design for Recombinant Protein Production in Tobacco.Biodesign research · 2024Review
- Development of a dual immunochromatographic test strip to detect E2 and EFrontiers in microbiology · 2024Article
- Rice-produced classical swine fever virus glycoprotein E2 with herringbone-dimer design to enhance immune responses.Plant biotechnology journal · 2023Article
- Recent advances in expression and purification strategies for plant made vaccines.Frontiers in plant science · 2023Review
- Review
- Production of Recombinant Active Human TGFβ1 inFrontiers in plant science · 2022Article
- The next-generation coronavirus diagnostic techniques with particular emphasis on the SARS-CoV-2.Journal of medical virology · 2021Review
- Article
- Research Progress and Challenges in Vaccine Development against Classical Swine Fever Virus.Viruses · 2021Review
- Future perspectives on swine viral vaccines: where are we headed?Porcine health management · 2021Review
- Development of Plant-Produced Recombinant ACE2-Fc Fusion Protein as a Potential Therapeutic Agent Against SARS-CoV-2.Frontiers in plant science · 2020Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Classical swine fever (CSF) is one of the most important viral diseases of swine worldwide. Although live or attenuated virus vaccines have been used to control CSFV, it is difficult to distinguish vaccinated pigs from infected pigs; this leads to restrictions on import and export. Subunit vaccines based on the CSFV E2 glycoprotein have been developed using baculovirus or insect cell systems, but some weaknesses remain. Here, we describe production of an E2 recombinant protein using a Nicotiana benthamiana plant expression system. To do this, we took advantage of the ability of the swine Fc domain to increase solubility and stability of the fusion protein and to strengthen immune responses in target animals. N. benthamiana expressed high amounts of pFc2-fused E2 proteins, which were isolated and purified by affinity chromatography to yield a high pure recombinant protein in a cost-effective manner. Native-polyacrylamide gel electrophoresis and size exclusion chromatography confirmed that the pmE2:pFc2 fusion exists as a multimer rather than as a dimer. Injection of recombinant pmE2 protein into mice or piglets generated anti-pmE2 antibodies with efficient neutralizing activity against CSFV. These results suggest that a purified recombinant E2 protein produced in N. benthamiana generates high titers of neutralizing antibodies in vivo; as such, the protein could be developed as a subunit vaccine against CSFV.
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