Enhanced production of full-length immunoglobulin G via the signal recognition particle (SRP)-dependent pathway in Escherichia coli

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dc.contributor.authorLee, Yong Jaeko
dc.contributor.authorKim, Hee Sungko
dc.contributor.authorRyu, Ae Jinko
dc.contributor.authorJeong, Kijunko
dc.date.accessioned2013-07-18T06:59:33Z-
dc.date.available2013-07-18T06:59:33Z-
dc.date.created2013-07-03-
dc.date.created2013-07-03-
dc.date.issued2013-05-
dc.identifier.citationJOURNAL OF BIOTECHNOLOGY, v.165, no.2, pp.102 - 108-
dc.identifier.issn0168-1656-
dc.identifier.urihttp://hdl.handle.net/10203/174036-
dc.description.abstractBecause of the lack of post-translational glycosylation, Escherichia coil is not a preferable host for immunoglobulin G (IgG) production. However, recent successes in the developments of aglycosylated IgG variants that do not require glycosylation for effector functions have increased the likelihood of using E. coil for IgG production. Here, we have developed a new E. coil host-vector system for enhanced production of recombinant IgG using: (i) a combination of SRP/Sec-dependent pathways for the efficient secretion of heavy and light chains in the periplasm; (ii) co-expression of periplasmic foldase (DsbC) for efficient assembly of IgG in the periplasm; and (iii) co-expression of Ffh for enhancing the SRP machinery. Finally, with engineered host-vector system, fed-batch cultivations were conducted at four different conditions, and under an optimized condition, up to 62 mg/L of active full-length IgG was produced during a 28-h cultivation. (C) 2013 Elsevier B.V. All rights reserved.-
dc.languageEnglish-
dc.publisherELSEVIER SCIENCE BV-
dc.subjectDISULFIDE BOND FORMATION-
dc.subjectHIGH-LEVEL EXPRESSION-
dc.subjectANTIBODIES-
dc.subjectPROTEIN-
dc.subjectGLYCOSYLATION-
dc.subjectTRANSLOCATION-
dc.subjectSTRATEGIES-
dc.subjectMEMBRANE-
dc.subjectCULTURE-
dc.titleEnhanced production of full-length immunoglobulin G via the signal recognition particle (SRP)-dependent pathway in Escherichia coli-
dc.typeArticle-
dc.identifier.wosid000319244000005-
dc.identifier.scopusid2-s2.0-84876717271-
dc.type.rimsART-
dc.citation.volume165-
dc.citation.issue2-
dc.citation.beginningpage102-
dc.citation.endingpage108-
dc.citation.publicationnameJOURNAL OF BIOTECHNOLOGY-
dc.identifier.doi10.1016/j.jbiotec.2013.03.007-
dc.contributor.localauthorJeong, Kijun-
dc.contributor.nonIdAuthorLee, Yong Jae-
dc.contributor.nonIdAuthorKim, Hee Sung-
dc.contributor.nonIdAuthorRyu, Ae Jin-
dc.type.journalArticleArticle-
dc.subject.keywordAuthorEscherichia coli-
dc.subject.keywordAuthorImmunoglobulin G-
dc.subject.keywordAuthorSRP pathway-
dc.subject.keywordAuthorFed-batch cultivation-
dc.subject.keywordPlusDISULFIDE BOND FORMATION-
dc.subject.keywordPlusHIGH-LEVEL EXPRESSION-
dc.subject.keywordPlusANTIBODIES-
dc.subject.keywordPlusPROTEIN-
dc.subject.keywordPlusGLYCOSYLATION-
dc.subject.keywordPlusTRANSLOCATION-
dc.subject.keywordPlusSTRATEGIES-
dc.subject.keywordPlusMEMBRANE-
dc.subject.keywordPlusCULTURE-
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