Translocation from the chloroplast stroma into the thylakoid lumen allows expression of recombinant epidermal growth factor in transplastomic tobacco plants.
Identifieur interne : 000004 ( Main/Exploration ); précédent : 000003; suivant : 000005Translocation from the chloroplast stroma into the thylakoid lumen allows expression of recombinant epidermal growth factor in transplastomic tobacco plants.
Auteurs : Mauro M. Morgenfeld [Argentine] ; Catalina F. Vater [Argentine] ; E Federico Alfano [Argentine] ; Noelia A. Boccardo [Argentine] ; Fernando F. Bravo-Almonacid [Argentine]Source :
- Transgenic research [ 1573-9368 ] ; 2020.
Abstract
Chloroplast transformation has many potential advantages for the production of recombinant proteins in plants. However, it has been reported that chloroplast expression of many proteins, such as human epidermal growth factor (hEGF), results hindered by post-transcriptional mechanisms. hEGF degradation has been related to the redox potential of the stroma and protein misfolding. To solve this problem, we proposed the redirection of hEGF into the thylakoid lumen where the environment could improve disulfide bonds formation stabilizing the functional conformation of the protein. We generated transplastomic tobacco plants targeting hEGF protein to the thylakoid lumen by adding a transit peptide (Str). Following this approach, we could detect thylakoid lumen-targeted hEGF by western blotting while stromal accumulation of hEGF remained undetectable. Southern blot analysis confirmed the integration of the transgene through homologous recombination into the plastome. Northern blot analysis showed similar levels of egf transcripts in the EGF and StrEGF lines. These results suggest that higher stability of the hEGF peptide in the thylakoid lumen is the primary cause of the increased accumulation of the recombinant protein observed in StrEGF lines. They also highlight the necessity of exploring different sub-organellar destinations to improve the accumulation levels of a specific recombinant protein in plastids.
DOI: 10.1007/s11248-020-00199-7
PubMed: 32318934
Affiliations:
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Morgenfeld</name><affiliation wicri:level="1"><nlm:affiliation>Instituto de Ingeniería Genética y Biología Molecular "Dr, Héctor Torres" (INGEBI-CONICET), Vuelta de Obligado 2490, Ciudad Autónoma de Buenos Aires, Argentina.</nlm:affiliation><country xml:lang="fr">Argentine</country><wicri:regionArea>Instituto de Ingeniería Genética y Biología Molecular "Dr, Héctor Torres" (INGEBI-CONICET), Vuelta de Obligado 2490, Ciudad Autónoma de Buenos Aires</wicri:regionArea><wicri:noRegion>Ciudad Autónoma de Buenos Aires</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Departamento de Fisiología, Biología Molecular y Celular (FCEN-UBA), Buenos Aires, Argentina.</nlm:affiliation><country xml:lang="fr">Argentine</country><wicri:regionArea>Departamento de Fisiología, Biología Molecular y Celular (FCEN-UBA), Buenos Aires</wicri:regionArea><wicri:noRegion>Buenos Aires</wicri:noRegion></affiliation></author><author><name sortKey="Vater, Catalina F" sort="Vater, Catalina F" uniqKey="Vater C" first="Catalina F" last="Vater">Catalina F. Vater</name><affiliation wicri:level="1"><nlm:affiliation>Instituto de Ingeniería Genética y Biología Molecular "Dr, Héctor Torres" (INGEBI-CONICET), Vuelta de Obligado 2490, Ciudad Autónoma de Buenos Aires, Argentina.</nlm:affiliation><country xml:lang="fr">Argentine</country><wicri:regionArea>Instituto de Ingeniería Genética y Biología Molecular "Dr, Héctor Torres" (INGEBI-CONICET), Vuelta de Obligado 2490, Ciudad Autónoma de Buenos Aires</wicri:regionArea><wicri:noRegion>Ciudad Autónoma de Buenos Aires</wicri:noRegion></affiliation></author><author><name sortKey="Alfano, E Federico" sort="Alfano, E Federico" uniqKey="Alfano E" first="E Federico" last="Alfano">E Federico Alfano</name><affiliation wicri:level="1"><nlm:affiliation>Instituto de Ingeniería Genética y Biología Molecular "Dr, Héctor Torres" (INGEBI-CONICET), Vuelta de Obligado 2490, Ciudad Autónoma de Buenos Aires, Argentina.</nlm:affiliation><country xml:lang="fr">Argentine</country><wicri:regionArea>Instituto de Ingeniería Genética y Biología Molecular "Dr, Héctor Torres" (INGEBI-CONICET), Vuelta de Obligado 2490, Ciudad Autónoma de Buenos Aires</wicri:regionArea><wicri:noRegion>Ciudad Autónoma de Buenos Aires</wicri:noRegion></affiliation></author><author><name sortKey="Boccardo, Noelia A" sort="Boccardo, Noelia A" uniqKey="Boccardo N" first="Noelia A" last="Boccardo">Noelia A. Boccardo</name><affiliation wicri:level="1"><nlm:affiliation>Instituto de Ingeniería Genética y Biología Molecular "Dr, Héctor Torres" (INGEBI-CONICET), Vuelta de Obligado 2490, Ciudad Autónoma de Buenos Aires, Argentina.</nlm:affiliation><country xml:lang="fr">Argentine</country><wicri:regionArea>Instituto de Ingeniería Genética y Biología Molecular "Dr, Héctor Torres" (INGEBI-CONICET), Vuelta de Obligado 2490, Ciudad Autónoma de Buenos Aires</wicri:regionArea><wicri:noRegion>Ciudad Autónoma de Buenos Aires</wicri:noRegion></affiliation></author><author><name sortKey="Bravo Almonacid, Fernando F" sort="Bravo Almonacid, Fernando F" uniqKey="Bravo Almonacid F" first="Fernando F" last="Bravo-Almonacid">Fernando F. Bravo-Almonacid</name><affiliation wicri:level="1"><nlm:affiliation>Instituto de Ingeniería Genética y Biología Molecular "Dr, Héctor Torres" (INGEBI-CONICET), Vuelta de Obligado 2490, Ciudad Autónoma de Buenos Aires, Argentina. fbravo@dna.uba.ar.</nlm:affiliation><country xml:lang="fr">Argentine</country><wicri:regionArea>Instituto de Ingeniería Genética y Biología Molecular "Dr, Héctor Torres" (INGEBI-CONICET), Vuelta de Obligado 2490, Ciudad Autónoma de Buenos Aires</wicri:regionArea><wicri:noRegion>Ciudad Autónoma de Buenos Aires</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Bernal, Buenos Aires, Argentina. fbravo@dna.uba.ar.</nlm:affiliation><country xml:lang="fr">Argentine</country><wicri:regionArea>Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Bernal, Buenos Aires</wicri:regionArea><wicri:noRegion>Buenos Aires</wicri:noRegion></affiliation></author></analytic><series><title level="j">Transgenic research</title><idno type="eISSN">1573-9368</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Chloroplast transformation has many potential advantages for the production of recombinant proteins in plants. However, it has been reported that chloroplast expression of many proteins, such as human epidermal growth factor (hEGF), results hindered by post-transcriptional mechanisms. hEGF degradation has been related to the redox potential of the stroma and protein misfolding. To solve this problem, we proposed the redirection of hEGF into the thylakoid lumen where the environment could improve disulfide bonds formation stabilizing the functional conformation of the protein. We generated transplastomic tobacco plants targeting hEGF protein to the thylakoid lumen by adding a transit peptide (Str). Following this approach, we could detect thylakoid lumen-targeted hEGF by western blotting while stromal accumulation of hEGF remained undetectable. Southern blot analysis confirmed the integration of the transgene through homologous recombination into the plastome. Northern blot analysis showed similar levels of egf transcripts in the EGF and StrEGF lines. These results suggest that higher stability of the hEGF peptide in the thylakoid lumen is the primary cause of the increased accumulation of the recombinant protein observed in StrEGF lines. They also highlight the necessity of exploring different sub-organellar destinations to improve the accumulation levels of a specific recombinant protein in plastids.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">32318934</PMID><DateRevised><Year>2020</Year><Month>08</Month><Day>17</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1573-9368</ISSN><JournalIssue CitedMedium="Internet"><Volume>29</Volume><Issue>3</Issue><PubDate><Year>2020</Year><Month>06</Month></PubDate></JournalIssue><Title>Transgenic research</Title><ISOAbbreviation>Transgenic Res</ISOAbbreviation></Journal><ArticleTitle>Translocation from the chloroplast stroma into the thylakoid lumen allows expression of recombinant epidermal growth factor in transplastomic tobacco plants.</ArticleTitle><Pagination><MedlinePgn>295-305</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s11248-020-00199-7</ELocationID><Abstract><AbstractText>Chloroplast transformation has many potential advantages for the production of recombinant proteins in plants. However, it has been reported that chloroplast expression of many proteins, such as human epidermal growth factor (hEGF), results hindered by post-transcriptional mechanisms. hEGF degradation has been related to the redox potential of the stroma and protein misfolding. To solve this problem, we proposed the redirection of hEGF into the thylakoid lumen where the environment could improve disulfide bonds formation stabilizing the functional conformation of the protein. We generated transplastomic tobacco plants targeting hEGF protein to the thylakoid lumen by adding a transit peptide (Str). Following this approach, we could detect thylakoid lumen-targeted hEGF by western blotting while stromal accumulation of hEGF remained undetectable. Southern blot analysis confirmed the integration of the transgene through homologous recombination into the plastome. Northern blot analysis showed similar levels of egf transcripts in the EGF and StrEGF lines. These results suggest that higher stability of the hEGF peptide in the thylakoid lumen is the primary cause of the increased accumulation of the recombinant protein observed in StrEGF lines. They also highlight the necessity of exploring different sub-organellar destinations to improve the accumulation levels of a specific recombinant protein in plastids.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Morgenfeld</LastName><ForeName>Mauro M</ForeName><Initials>MM</Initials><AffiliationInfo><Affiliation>Instituto de Ingeniería Genética y Biología Molecular "Dr, Héctor Torres" (INGEBI-CONICET), Vuelta de Obligado 2490, Ciudad Autónoma de Buenos Aires, Argentina.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Departamento de Fisiología, Biología Molecular y Celular (FCEN-UBA), Buenos Aires, Argentina.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Vater</LastName><ForeName>Catalina F</ForeName><Initials>CF</Initials><AffiliationInfo><Affiliation>Instituto de Ingeniería Genética y Biología Molecular "Dr, Héctor Torres" (INGEBI-CONICET), Vuelta de Obligado 2490, Ciudad Autónoma de Buenos Aires, Argentina.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Alfano</LastName><ForeName>E Federico</ForeName><Initials>EF</Initials><AffiliationInfo><Affiliation>Instituto de Ingeniería Genética y Biología Molecular "Dr, Héctor Torres" (INGEBI-CONICET), Vuelta de Obligado 2490, Ciudad Autónoma de Buenos Aires, Argentina.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Boccardo</LastName><ForeName>Noelia A</ForeName><Initials>NA</Initials><AffiliationInfo><Affiliation>Instituto de Ingeniería Genética y Biología Molecular "Dr, Héctor Torres" (INGEBI-CONICET), Vuelta de Obligado 2490, Ciudad Autónoma de Buenos Aires, Argentina.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bravo-Almonacid</LastName><ForeName>Fernando F</ForeName><Initials>FF</Initials><Identifier Source="ORCID">0000-0002-7102-3109</Identifier><AffiliationInfo><Affiliation>Instituto de Ingeniería Genética y Biología Molecular "Dr, Héctor Torres" (INGEBI-CONICET), Vuelta de Obligado 2490, Ciudad Autónoma de Buenos Aires, Argentina. fbravo@dna.uba.ar.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Bernal, Buenos Aires, Argentina. fbravo@dna.uba.ar.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>2013-1355</GrantID><Agency>Fondo para la Investigación Científica y Tecnológica</Agency><Country>International</Country></Grant><Grant><GrantID>2014-2766</GrantID><Agency>Fondo para la Investigación Científica y Tecnológica</Agency><Country>International</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>04</Month><Day>21</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Transgenic Res</MedlineTA><NlmUniqueID>9209120</NlmUniqueID><ISSNLinking>0962-8819</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Human epidermal growth factor, EGF</Keyword><Keyword MajorTopicYN="Y">Molecular farming</Keyword><Keyword MajorTopicYN="Y">Thylakoid</Keyword><Keyword MajorTopicYN="Y">Translocation</Keyword><Keyword MajorTopicYN="Y">Transplastomic tobacco</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>02</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>04</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>4</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>4</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>4</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32318934</ArticleId><ArticleId IdType="doi">10.1007/s11248-020-00199-7</ArticleId><ArticleId IdType="pii">10.1007/s11248-020-00199-7</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Argentine</li></country></list><tree><country name="Argentine"><noRegion><name sortKey="Morgenfeld, Mauro M" sort="Morgenfeld, Mauro M" uniqKey="Morgenfeld M" first="Mauro M" last="Morgenfeld">Mauro M. Morgenfeld</name></noRegion><name sortKey="Alfano, E Federico" sort="Alfano, E Federico" uniqKey="Alfano E" first="E Federico" last="Alfano">E Federico Alfano</name><name sortKey="Boccardo, Noelia A" sort="Boccardo, Noelia A" uniqKey="Boccardo N" first="Noelia A" last="Boccardo">Noelia A. Boccardo</name><name sortKey="Bravo Almonacid, Fernando F" sort="Bravo Almonacid, Fernando F" uniqKey="Bravo Almonacid F" first="Fernando F" last="Bravo-Almonacid">Fernando F. Bravo-Almonacid</name><name sortKey="Bravo Almonacid, Fernando F" sort="Bravo Almonacid, Fernando F" uniqKey="Bravo Almonacid F" first="Fernando F" last="Bravo-Almonacid">Fernando F. Bravo-Almonacid</name><name sortKey="Morgenfeld, Mauro M" sort="Morgenfeld, Mauro M" uniqKey="Morgenfeld M" first="Mauro M" last="Morgenfeld">Mauro M. Morgenfeld</name><name sortKey="Vater, Catalina F" sort="Vater, Catalina F" uniqKey="Vater C" first="Catalina F" last="Vater">Catalina F. 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