Expression of a multi-epitope DPT fusion protein in transplastomic tobacco plants retains both antigenicity and immunogenicity of all three components of the functional oligomer
Identifieur interne : 001A72 ( Istex/Corpus ); précédent : 001A71; suivant : 001A73Expression of a multi-epitope DPT fusion protein in transplastomic tobacco plants retains both antigenicity and immunogenicity of all three components of the functional oligomer
Auteurs : Ruth Elena Soria-Guerra ; Angel G. Alpuche-Solís ; Sergio Rosales-Mendoza ; Leticia Moreno-Fierros ; Elise M. Bendik ; Luzmila Martínez-González ; Schuyler S. KorbanSource :
- Planta [ 0032-0935 ] ; 2009-05-01.
English descriptors
Abstract
Abstract: Expression of genes in plant chloroplasts provides an opportunity for enhanced production of target proteins. We report the introduction and expression of a fusion DPT protein containing immunoprotective exotoxin epitopes of Corynebacterium diphtheriae, Bordetella pertussis, and Clostridium tetani in tobacco chloroplasts. Using biolistic-mediated transformation, a plant-optimized synthetic DPT gene was successfully transferred to tobacco plastomes. Putative transplastomic T0 plants were identified by PCR, and Southern blot analysis confirmed homoplasmy in T1 progeny. ELISA assays demonstrated that the DPT protein retained antigenicity of the three components of the fusion protein. The highest level of expression in these transplastomic plants reached 0.8% of total soluble protein. To assess whether the functional recombinant protein expressed in tobacco plants would induce specific antibodies in test animals, a mice feeding experiment was conducted. For mice orally immunized with freeze-dried transplastomic leaves, production of IgG and IgA antibodies specific to each toxin were detected in serum and mucosal tissues.
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DOI: 10.1007/s00425-009-0918-2
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We report the introduction and expression of a fusion DPT protein containing immunoprotective exotoxin epitopes of Corynebacterium diphtheriae, Bordetella pertussis, and Clostridium tetani in tobacco chloroplasts. Using biolistic-mediated transformation, a plant-optimized synthetic DPT gene was successfully transferred to tobacco plastomes. Putative transplastomic T0 plants were identified by PCR, and Southern blot analysis confirmed homoplasmy in T1 progeny. ELISA assays demonstrated that the DPT protein retained antigenicity of the three components of the fusion protein. The highest level of expression in these transplastomic plants reached 0.8% of total soluble protein. To assess whether the functional recombinant protein expressed in tobacco plants would induce specific antibodies in test animals, a mice feeding experiment was conducted. For mice orally immunized with freeze-dried transplastomic leaves, production of IgG and IgA antibodies specific to each toxin were detected in serum and mucosal tissues.</div></front></TEI><istex><corpusName>springer-journals</corpusName><author><json:item><name>Ruth Elena Soria-Guerra</name><affiliations><json:string>Department of Natural Resources and Environmental Sciences, University of Illinois, 61821, Urbana, IL, USA</json:string></affiliations></json:item><json:item><name>Angel G. 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We report the introduction and expression of a fusion DPT protein containing immunoprotective exotoxin epitopes of Corynebacterium diphtheriae, Bordetella pertussis, and Clostridium tetani in tobacco chloroplasts. Using biolistic-mediated transformation, a plant-optimized synthetic DPT gene was successfully transferred to tobacco plastomes. Putative transplastomic T0 plants were identified by PCR, and Southern blot analysis confirmed homoplasmy in T1 progeny. ELISA assays demonstrated that the DPT protein retained antigenicity of the three components of the fusion protein. The highest level of expression in these transplastomic plants reached 0.8% of total soluble protein. To assess whether the functional recombinant protein expressed in tobacco plants would induce specific antibodies in test animals, a mice feeding experiment was conducted. 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the functional oligomer</ArticleTitle><ArticleCategory>Original Article</ArticleCategory><ArticleFirstPage>1293</ArticleFirstPage><ArticleLastPage>1302</ArticleLastPage><ArticleHistory><RegistrationDate><Year>2009</Year><Month>3</Month><Day>6</Day></RegistrationDate><Received><Year>2009</Year><Month>2</Month><Day>2</Day></Received><Accepted><Year>2009</Year><Month>3</Month><Day>4</Day></Accepted><OnlineDate><Year>2009</Year><Month>3</Month><Day>21</Day></OnlineDate></ArticleHistory><ArticleCopyright><CopyrightHolderName>Springer-Verlag</CopyrightHolderName><CopyrightYear>2009</CopyrightYear></ArticleCopyright><ArticleGrants Type="Regular"><MetadataGrant Grant="OpenAccess"></MetadataGrant><AbstractGrant Grant="OpenAccess"></AbstractGrant><BodyPDFGrant Grant="Restricted"></BodyPDFGrant><BodyHTMLGrant Grant="Restricted"></BodyHTMLGrant><BibliographyGrant Grant="Restricted"></BibliographyGrant><ESMGrant Grant="Restricted"></ESMGrant></ArticleGrants></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Ruth</GivenName><GivenName>Elena</GivenName><FamilyName>Soria-Guerra</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>Angel</GivenName><GivenName>G.</GivenName><FamilyName>Alpuche-Solís</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Sergio</GivenName><FamilyName>Rosales-Mendoza</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff3"><AuthorName DisplayOrder="Western"><GivenName>Leticia</GivenName><FamilyName>Moreno-Fierros</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Elise</GivenName><GivenName>M.</GivenName><FamilyName>Bendik</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>Luzmila</GivenName><FamilyName>Martínez-González</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1 Aff4" CorrespondingAffiliationID="Aff4"><AuthorName DisplayOrder="Western"><GivenName>Schuyler</GivenName><GivenName>S.</GivenName><FamilyName>Korban</FamilyName></AuthorName><Contact><Email>korban@illinois.edu</Email></Contact></Author><Affiliation ID="Aff1"><OrgDivision>Department of Natural Resources and Environmental Sciences</OrgDivision><OrgName>University of Illinois</OrgName><OrgAddress><City>Urbana</City><State>IL</State><Postcode>61821</Postcode><Country Code="US">USA</Country></OrgAddress></Affiliation><Affiliation ID="Aff2"><OrgDivision>División de Biología Molecular</OrgDivision><OrgName>Instituto Potosino de Investigación Científica y Tecnológica</OrgName><OrgAddress><Street>Camino a la Presa San José 2055</Street><Postcode>78216</Postcode><City>San Luis Potosí</City><Country Code="MX">Mexico</Country></OrgAddress></Affiliation><Affiliation ID="Aff3"><OrgDivision>Inmunidad en Mucosas, UBIMED, FES-Iztacala</OrgDivision><OrgName>Universidad Nacional Autónoma de México</OrgName><OrgAddress><Street>Avenida de los Barrios 1, Los Reyes Iztacala</Street><Postcode>54090</Postcode><City>Tlalnepantla</City><Country Code="MX">Mexico</Country></OrgAddress></Affiliation><Affiliation ID="Aff4"><OrgName>University of Illinois at Urbana-Champaign</OrgName><OrgAddress><City>Urbana</City><State>IL</State><Postcode>61801</Postcode><Country Code="US">USA</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En" OutputMedium="All"><Heading>Abstract</Heading><Para>Expression of genes in plant chloroplasts provides an opportunity for enhanced production of target proteins. We report the introduction and expression of a fusion DPT protein containing immunoprotective exotoxin epitopes of <Emphasis Type="Italic">Corynebacterium</Emphasis> <Emphasis Type="Italic">diphtheriae</Emphasis>, <Emphasis Type="Italic">Bordetella</Emphasis> <Emphasis Type="Italic">pertussis</Emphasis>, and <Emphasis Type="Italic">Clostridium</Emphasis> <Emphasis Type="Italic">tetani</Emphasis> in tobacco chloroplasts. Using biolistic-mediated transformation, a plant-optimized synthetic <Emphasis Type="Italic">DPT</Emphasis> gene was successfully transferred to tobacco plastomes. Putative transplastomic T0 plants were identified by PCR, and Southern blot analysis confirmed homoplasmy in T1 progeny. ELISA assays demonstrated that the DPT protein retained antigenicity of the three components of the fusion protein. The highest level of expression in these transplastomic plants reached 0.8% of total soluble protein. To assess whether the functional recombinant protein expressed in tobacco plants would induce specific antibodies in test animals, a mice feeding experiment was conducted. For mice orally immunized with freeze-dried transplastomic leaves, production of IgG and IgA antibodies specific to each toxin were detected in serum and mucosal tissues.</Para></Abstract><KeywordGroup Language="En" OutputMedium="All"><Heading>Keywords</Heading><Keyword>Plastid expression</Keyword><Keyword>Transplastomic plants</Keyword><Keyword>DPT recombinant protein</Keyword><Keyword>Immunogenic polypeptide</Keyword></KeywordGroup><ArticleNote Type="Misc"><SimplePara>R. E. Soria-Guerra and A. G. Alpuche-Solís contributed equally to this work.</SimplePara></ArticleNote></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Expression of a multi-epitope DPT fusion protein in transplastomic tobacco plants retains both antigenicity and immunogenicity of all three components of the functional oligomer</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Expression of a multi-epitope DPT fusion protein in transplastomic tobacco plants retains both antigenicity and immunogenicity of all three components of the functional oligomer</title></titleInfo><name type="personal"><namePart type="given">Ruth</namePart><namePart type="given">Elena</namePart><namePart type="family">Soria-Guerra</namePart><affiliation>Department of Natural Resources and Environmental Sciences, University of Illinois, 61821, Urbana, IL, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Angel</namePart><namePart type="given">G.</namePart><namePart type="family">Alpuche-Solís</namePart><affiliation>División de Biología Molecular, Instituto Potosino de Investigación Científica y Tecnológica, Camino a la Presa San José 2055, 78216, San Luis Potosí, Mexico</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Sergio</namePart><namePart type="family">Rosales-Mendoza</namePart><affiliation>Department of Natural Resources and Environmental Sciences, University of Illinois, 61821, Urbana, IL, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Leticia</namePart><namePart type="family">Moreno-Fierros</namePart><affiliation>Inmunidad en Mucosas, UBIMED, FES-Iztacala, Universidad Nacional Autónoma de México, Avenida de los Barrios 1, Los Reyes Iztacala, 54090, Tlalnepantla, Mexico</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Elise</namePart><namePart type="given">M.</namePart><namePart type="family">Bendik</namePart><affiliation>Department of Natural Resources and Environmental Sciences, University of Illinois, 61821, Urbana, IL, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Luzmila</namePart><namePart type="family">Martínez-González</namePart><affiliation>División de Biología Molecular, Instituto Potosino de Investigación Científica y Tecnológica, Camino a la Presa San José 2055, 78216, San Luis Potosí, Mexico</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal" displayLabel="corresp"><namePart type="given">Schuyler</namePart><namePart type="given">S.</namePart><namePart type="family">Korban</namePart><affiliation>Department of Natural Resources and Environmental Sciences, University of Illinois, 61821, Urbana, IL, USA</affiliation><affiliation>University of Illinois at Urbana-Champaign, 61801, Urbana, IL, USA</affiliation><affiliation>E-mail: korban@illinois.edu</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="OriginalPaper" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>Springer-Verlag</publisher><place><placeTerm type="text">Berlin/Heidelberg</placeTerm></place><dateCreated encoding="w3cdtf">2009-02-02</dateCreated><dateIssued encoding="w3cdtf">2009-05-01</dateIssued><copyrightDate encoding="w3cdtf">2009</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Abstract: Expression of genes in plant chloroplasts provides an opportunity for enhanced production of target proteins. We report the introduction and expression of a fusion DPT protein containing immunoprotective exotoxin epitopes of Corynebacterium diphtheriae, Bordetella pertussis, and Clostridium tetani in tobacco chloroplasts. Using biolistic-mediated transformation, a plant-optimized synthetic DPT gene was successfully transferred to tobacco plastomes. Putative transplastomic T0 plants were identified by PCR, and Southern blot analysis confirmed homoplasmy in T1 progeny. ELISA assays demonstrated that the DPT protein retained antigenicity of the three components of the fusion protein. The highest level of expression in these transplastomic plants reached 0.8% of total soluble protein. To assess whether the functional recombinant protein expressed in tobacco plants would induce specific antibodies in test animals, a mice feeding experiment was conducted. For mice orally immunized with freeze-dried transplastomic leaves, production of IgG and IgA antibodies specific to each toxin were detected in serum and mucosal tissues.</abstract><note>Original Article</note><subject lang="en"><genre>Keywords</genre><topic>Plastid expression</topic><topic>Transplastomic plants</topic><topic>DPT recombinant protein</topic><topic>Immunogenic polypeptide</topic></subject><relatedItem type="host"><titleInfo><title>Planta</title><subTitle>An International Journal of Plant Biology</subTitle></titleInfo><titleInfo type="abbreviated"><title>Planta</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>Springer</publisher><dateIssued encoding="w3cdtf">2009-04-26</dateIssued><copyrightDate encoding="w3cdtf">2009</copyrightDate></originInfo><subject><genre>Life Sciences</genre><topic>Ecology</topic><topic>Forestry</topic><topic>Agriculture</topic><topic>Plant Sciences</topic></subject><identifier type="ISSN">0032-0935</identifier><identifier type="eISSN">1432-2048</identifier><identifier type="JournalID">425</identifier><identifier type="IssueArticleCount">17</identifier><identifier type="VolumeIssueCount">6</identifier><part><date>2009</date><detail type="volume"><number>229</number><caption>vol.</caption></detail><detail type="issue"><number>6</number><caption>no.</caption></detail><extent unit="pages"><start>1293</start><end>1302</end></extent></part><recordInfo><recordOrigin>Springer-Verlag, 2009</recordOrigin></recordInfo></relatedItem><identifier type="istex">8E45C94FDC0B7D8B1D732065350EB09CCD96922D</identifier><identifier type="ark">ark:/67375/VQC-FDJ1QGZM-V</identifier><identifier type="DOI">10.1007/s00425-009-0918-2</identifier><identifier type="ArticleID">918</identifier><identifier type="ArticleID">s00425-009-0918-2</identifier><accessCondition type="use and reproduction" contentType="copyright">Springer-Verlag, 2009</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-3XSW68JL-F">springer</recordContentSource><recordOrigin>Springer-Verlag, 2009</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-FDJ1QGZM-V/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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