Immunogenicity of a neutralizing epitope from porcine epidemic diarrhea virus: M cell targeting ligand fusion protein expressed in transgenic rice calli
Identifieur interne : 001E75 ( Main/Exploration ); précédent : 001E74; suivant : 001E76Immunogenicity of a neutralizing epitope from porcine epidemic diarrhea virus: M cell targeting ligand fusion protein expressed in transgenic rice calli
Auteurs : Nguyen-Xuan Huy [Corée du Sud, Viêt Nam] ; Sae-Hae Kim [Corée du Sud] ; Moon-Sik Yang [Corée du Sud] ; Tae-Geum Kim [Corée du Sud]Source :
- Plant Cell Reports [ 0721-7714 ] ; 2012-10-01.
English descriptors
Abstract
Abstract: To increase immune responses of plant-based vaccines in intestine mucosal immune systems, a synthetic neutralizing epitope (sCOE) gene of porcine epidemic diarrhea virus (PEDV) was fused with M cell-targeting ligand (Co1) and introduced into a plant expression vector under the control of rice amylase 3D promoter. The sCOE–Co1 fusion gene was introduced into rice calli via the particle bombardment-mediated transformation method. The stable integration and transcriptional expression of the sCOE–Co1 fusion gene was confirmed by genomic DNA PCR amplification and Northern blot analysis, respectively. The expression of the COE–Co1 fusion protein was confirmed by immunoblot analysis. The highest expression level of the COE–Co1 fusion protein reached 0.083 % of the total soluble protein according to quantitative densitometry of Western blot analysis. Mice immunized with transgenic rice calli protein extracts induced significant serum IgG and fecal IgA antibody levels against purified bacterial COE. The systemic and mucosal immune responses were confirmed by measuring COE-specific IgG and IgA antibody-secreting cells in the lymphocytes extracted from the spleen and COE-specific IgA antibody-secreting cells in the Peyer’s patches from immunized mice. These results indicated that oral immunization of plant-produced COE–Co1 fusion protein could elicit efficient systemic and mucosal immune responses against the COE antigen. Key message Neutralizing epitope from porcine epidemic diarrhea virus-M cell targeting ligand fusion protein was produced in transgenic rice calli and elicited systemic and mucosal immune responses by oral administration in mice.
Url:
DOI: 10.1007/s00299-012-1306-0
Affiliations:
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xml:lang="fr">Corée du Sud</country><wicri:regionArea>Research Center for Bioactive Materials, Chonbuk National University, 561-756, Jeonju</wicri:regionArea><wicri:noRegion>Jeonju</wicri:noRegion></affiliation><affiliation wicri:level="1"><country wicri:rule="url">Corée du Sud</country></affiliation></author></analytic><monogr></monogr><series><title level="j">Plant Cell Reports</title><title level="j" type="abbrev">Plant Cell Rep</title><idno type="ISSN">0721-7714</idno><idno type="eISSN">1432-203X</idno><imprint><publisher>Springer-Verlag</publisher><pubPlace>Berlin/Heidelberg</pubPlace><date type="published" when="2012-10-01">2012-10-01</date><biblScope unit="volume">31</biblScope><biblScope unit="issue">10</biblScope><biblScope unit="page" from="1933">1933</biblScope><biblScope unit="page" to="1942">1942</biblScope></imprint><idno type="ISSN">0721-7714</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0721-7714</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Edible vaccine</term><term>M cell-targeting ligand (Co1)</term><term>PEDV</term><term>Transgenic rice callus</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: To increase immune responses of plant-based vaccines in intestine mucosal immune systems, a synthetic neutralizing epitope (sCOE) gene of porcine epidemic diarrhea virus (PEDV) was fused with M cell-targeting ligand (Co1) and introduced into a plant expression vector under the control of rice amylase 3D promoter. The sCOE–Co1 fusion gene was introduced into rice calli via the particle bombardment-mediated transformation method. The stable integration and transcriptional expression of the sCOE–Co1 fusion gene was confirmed by genomic DNA PCR amplification and Northern blot analysis, respectively. The expression of the COE–Co1 fusion protein was confirmed by immunoblot analysis. The highest expression level of the COE–Co1 fusion protein reached 0.083 % of the total soluble protein according to quantitative densitometry of Western blot analysis. Mice immunized with transgenic rice calli protein extracts induced significant serum IgG and fecal IgA antibody levels against purified bacterial COE. The systemic and mucosal immune responses were confirmed by measuring COE-specific IgG and IgA antibody-secreting cells in the lymphocytes extracted from the spleen and COE-specific IgA antibody-secreting cells in the Peyer’s patches from immunized mice. These results indicated that oral immunization of plant-produced COE–Co1 fusion protein could elicit efficient systemic and mucosal immune responses against the COE antigen. 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