Expression and purification of soluble and functional fusion protein DAB389 IL-2 into the E. coli strain Rosetta-gami (DE3).
Identifieur interne : 000077 ( Main/Exploration ); précédent : 000076; suivant : 000078Expression and purification of soluble and functional fusion protein DAB389 IL-2 into the E. coli strain Rosetta-gami (DE3).
Auteurs : Nasrin Zarkar [Iran] ; Mohammad Ali Nasiri Khalili [Iran] ; Sirus Khodadadi [Iran] ; Mehdi Zeinoddini [Iran] ; Fathollah Ahmadpour [Iran]Source :
- Biotechnology and applied biochemistry [ 1470-8744 ] ; 2020.
Abstract
DAB389 IL-2 (Denileukin diftitox) is considered an immunotoxin, and it is the first immunotoxin approved by Food and Drug Administration. It is used for the treatment of a cutaneous form of T-cell lymphoma. This fusion protein has two disulfide bonds in its structure that play an essential role in toxicity and functionality of the immunotoxin. Escherichia coli (E. coli) strain BL21 (DE3) is not capable of making disulfide bonds in its reductive cytoplasm, but the E. coli strain Rosetta-gami (DE3) is a proper strain for the correct expression of the protein due to mutations in glutaredoxin reductase and thioredoxin reductase. In this study, a pET21a vector with the His6-tag fused at the N-terminus of DAB389 IL-2 was used to express the soluble immunotoxin in E. coli Rosetta-gami (DE3). After the purification of the soluble protein by two-step column chromatographies, the structure of DAB389 IL-2 was analyzed using the Native-PAGE and circular dichroism methods. In the following, the nuclease activity of soluble DAB389 IL-2 and its cytotoxicity activity were determined. It is concluded that the soluble recombinant protein expressed in the E. coli Rosetta-gami (DE3) has an intact structure and also functional; hence, this form of immunotoxin could be competitive with its commercial counterparts.
DOI: 10.1002/bab.1833
PubMed: 31600001
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xml:lang="fr">Iran</country><wicri:regionArea>Malek Ashtar University of Technology, Tehran</wicri:regionArea><wicri:noRegion>Tehran</wicri:noRegion></affiliation></author><author><name sortKey="Khodadadi, Sirus" sort="Khodadadi, Sirus" uniqKey="Khodadadi S" first="Sirus" last="Khodadadi">Sirus Khodadadi</name><affiliation wicri:level="1"><nlm:affiliation>Malek Ashtar University of Technology, Tehran, Iran.</nlm:affiliation><country xml:lang="fr">Iran</country><wicri:regionArea>Malek Ashtar University of Technology, Tehran</wicri:regionArea><wicri:noRegion>Tehran</wicri:noRegion></affiliation></author><author><name sortKey="Zeinoddini, Mehdi" sort="Zeinoddini, Mehdi" uniqKey="Zeinoddini M" first="Mehdi" last="Zeinoddini">Mehdi Zeinoddini</name><affiliation wicri:level="1"><nlm:affiliation>Malek Ashtar University of Technology, Tehran, Iran.</nlm:affiliation><country xml:lang="fr">Iran</country><wicri:regionArea>Malek Ashtar University of Technology, Tehran</wicri:regionArea><wicri:noRegion>Tehran</wicri:noRegion></affiliation></author><author><name sortKey="Ahmadpour, Fathollah" sort="Ahmadpour, Fathollah" uniqKey="Ahmadpour F" first="Fathollah" last="Ahmadpour">Fathollah Ahmadpour</name><affiliation wicri:level="1"><nlm:affiliation>Trauma Research Centre, Baqiyatallah University of Medical Sciences, Tehran, Iran.</nlm:affiliation><country xml:lang="fr">Iran</country><wicri:regionArea>Trauma Research Centre, Baqiyatallah University of Medical Sciences, Tehran</wicri:regionArea><wicri:noRegion>Tehran</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2020">2020</date><idno type="RBID">pubmed:31600001</idno><idno type="pmid">31600001</idno><idno type="doi">10.1002/bab.1833</idno><idno type="wicri:Area/Main/Corpus">000104</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000104</idno><idno 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Nasiri Khalili</name><affiliation wicri:level="1"><nlm:affiliation>Malek Ashtar University of Technology, Tehran, Iran.</nlm:affiliation><country xml:lang="fr">Iran</country><wicri:regionArea>Malek Ashtar University of Technology, Tehran</wicri:regionArea><wicri:noRegion>Tehran</wicri:noRegion></affiliation></author><author><name sortKey="Khodadadi, Sirus" sort="Khodadadi, Sirus" uniqKey="Khodadadi S" first="Sirus" last="Khodadadi">Sirus Khodadadi</name><affiliation wicri:level="1"><nlm:affiliation>Malek Ashtar University of Technology, Tehran, Iran.</nlm:affiliation><country xml:lang="fr">Iran</country><wicri:regionArea>Malek Ashtar University of Technology, Tehran</wicri:regionArea><wicri:noRegion>Tehran</wicri:noRegion></affiliation></author><author><name sortKey="Zeinoddini, Mehdi" sort="Zeinoddini, Mehdi" uniqKey="Zeinoddini M" first="Mehdi" last="Zeinoddini">Mehdi Zeinoddini</name><affiliation wicri:level="1"><nlm:affiliation>Malek Ashtar University of Technology, Tehran, Iran.</nlm:affiliation><country xml:lang="fr">Iran</country><wicri:regionArea>Malek Ashtar University of Technology, Tehran</wicri:regionArea><wicri:noRegion>Tehran</wicri:noRegion></affiliation></author><author><name sortKey="Ahmadpour, Fathollah" sort="Ahmadpour, Fathollah" uniqKey="Ahmadpour F" first="Fathollah" last="Ahmadpour">Fathollah Ahmadpour</name><affiliation wicri:level="1"><nlm:affiliation>Trauma Research Centre, Baqiyatallah University of Medical Sciences, Tehran, Iran.</nlm:affiliation><country xml:lang="fr">Iran</country><wicri:regionArea>Trauma Research Centre, Baqiyatallah University of Medical Sciences, Tehran</wicri:regionArea><wicri:noRegion>Tehran</wicri:noRegion></affiliation></author></analytic><series><title level="j">Biotechnology and applied biochemistry</title><idno type="eISSN">1470-8744</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">DAB<sub>389</sub> IL-2 (Denileukin diftitox) is considered an immunotoxin, and it is the first immunotoxin approved by Food and Drug Administration. It is used for the treatment of a cutaneous form of T-cell lymphoma. This fusion protein has two disulfide bonds in its structure that play an essential role in toxicity and functionality of the immunotoxin. Escherichia coli (E. coli) strain BL21 (DE3) is not capable of making disulfide bonds in its reductive cytoplasm, but the E. coli strain Rosetta-gami (DE3) is a proper strain for the correct expression of the protein due to mutations in glutaredoxin reductase and thioredoxin reductase. In this study, a pET21a vector with the His6-tag fused at the N-terminus of DAB<sub>389</sub> IL-2 was used to express the soluble immunotoxin in E. coli Rosetta-gami (DE3). After the purification of the soluble protein by two-step column chromatographies, the structure of DAB<sub>389</sub> IL-2 was analyzed using the Native-PAGE and circular dichroism methods. In the following, the nuclease activity of soluble DAB<sub>389</sub> IL-2 and its cytotoxicity activity were determined. It is concluded that the soluble recombinant protein expressed in the E. coli Rosetta-gami (DE3) has an intact structure and also functional; hence, this form of immunotoxin could be competitive with its commercial counterparts.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">31600001</PMID><DateRevised><Year>2020</Year><Month>06</Month><Day>12</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1470-8744</ISSN><JournalIssue CitedMedium="Internet"><Volume>67</Volume><Issue>2</Issue><PubDate><Year>2020</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Biotechnology and applied biochemistry</Title><ISOAbbreviation>Biotechnol Appl Biochem</ISOAbbreviation></Journal><ArticleTitle>Expression and purification of soluble and functional fusion protein DAB<sub>389</sub> IL-2 into the E. coli strain Rosetta-gami (DE3).</ArticleTitle><Pagination><MedlinePgn>206-212</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/bab.1833</ELocationID><Abstract><AbstractText>DAB<sub>389</sub> IL-2 (Denileukin diftitox) is considered an immunotoxin, and it is the first immunotoxin approved by Food and Drug Administration. It is used for the treatment of a cutaneous form of T-cell lymphoma. This fusion protein has two disulfide bonds in its structure that play an essential role in toxicity and functionality of the immunotoxin. Escherichia coli (E. coli) strain BL21 (DE3) is not capable of making disulfide bonds in its reductive cytoplasm, but the E. coli strain Rosetta-gami (DE3) is a proper strain for the correct expression of the protein due to mutations in glutaredoxin reductase and thioredoxin reductase. In this study, a pET21a vector with the His6-tag fused at the N-terminus of DAB<sub>389</sub> IL-2 was used to express the soluble immunotoxin in E. coli Rosetta-gami (DE3). After the purification of the soluble protein by two-step column chromatographies, the structure of DAB<sub>389</sub> IL-2 was analyzed using the Native-PAGE and circular dichroism methods. In the following, the nuclease activity of soluble DAB<sub>389</sub> IL-2 and its cytotoxicity activity were determined. It is concluded that the soluble recombinant protein expressed in the E. coli Rosetta-gami (DE3) has an intact structure and also functional; hence, this form of immunotoxin could be competitive with its commercial counterparts.</AbstractText><CopyrightInformation>© 2019 International Union of Biochemistry and Molecular Biology, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zarkar</LastName><ForeName>Nasrin</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Malek Ashtar University of Technology, Tehran, Iran.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nasiri Khalili</LastName><ForeName>Mohammad Ali</ForeName><Initials>MA</Initials><AffiliationInfo><Affiliation>Malek Ashtar University of Technology, Tehran, Iran.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Khodadadi</LastName><ForeName>Sirus</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Malek Ashtar University of Technology, Tehran, Iran.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zeinoddini</LastName><ForeName>Mehdi</ForeName><Initials>M</Initials><Identifier Source="ORCID">https://orcid.org/0000-0002-9500-1334</Identifier><AffiliationInfo><Affiliation>Malek Ashtar University of Technology, Tehran, Iran.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ahmadpour</LastName><ForeName>Fathollah</ForeName><Initials>F</Initials><Identifier Source="ORCID">https://orcid.org/0000-0003-2984-6897</Identifier><AffiliationInfo><Affiliation>Trauma Research Centre, Baqiyatallah University of Medical Sciences, Tehran, Iran.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>11</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biotechnol Appl Biochem</MedlineTA><NlmUniqueID>8609465</NlmUniqueID><ISSNLinking>0885-4513</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Rosetta-gami (DE3)</Keyword><Keyword MajorTopicYN="N">disulfide bond formation</Keyword><Keyword MajorTopicYN="N">immunotoxin</Keyword><Keyword MajorTopicYN="N">purification</Keyword><Keyword MajorTopicYN="N">soluble expression</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>02</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>09</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2019</Year><Month>10</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>10</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2019</Year><Month>10</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31600001</ArticleId><ArticleId IdType="doi">10.1002/bab.1833</ArticleId></ArticleIdList><ReferenceList><Title>References</Title><Reference><Citation>Strebhardt, K., and Ullrich, A. 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Methods 448, 51-58.</Citation></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Iran</li></country></list><tree><country name="Iran"><noRegion><name sortKey="Zarkar, Nasrin" sort="Zarkar, Nasrin" uniqKey="Zarkar N" first="Nasrin" last="Zarkar">Nasrin Zarkar</name></noRegion><name sortKey="Ahmadpour, Fathollah" sort="Ahmadpour, Fathollah" uniqKey="Ahmadpour F" first="Fathollah" last="Ahmadpour">Fathollah Ahmadpour</name><name sortKey="Khodadadi, Sirus" sort="Khodadadi, Sirus" uniqKey="Khodadadi S" first="Sirus" last="Khodadadi">Sirus Khodadadi</name><name sortKey="Nasiri Khalili, Mohammad Ali" sort="Nasiri Khalili, Mohammad Ali" uniqKey="Nasiri Khalili M" first="Mohammad Ali" last="Nasiri Khalili">Mohammad Ali Nasiri Khalili</name><name sortKey="Zeinoddini, Mehdi" sort="Zeinoddini, Mehdi" uniqKey="Zeinoddini M" first="Mehdi" last="Zeinoddini">Mehdi Zeinoddini</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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