Isolation of a Potential Anchoring Motif Based on Proteome Analysis of Escherichia coli and Its Use for Cell Surface Display

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dc.contributor.authorYim, Sung Sunko
dc.contributor.authorAn, Seul Jiko
dc.contributor.authorHan, Mee-Jungko
dc.contributor.authorChoi, Jae Woongko
dc.contributor.authorJeong, Kijunko
dc.date.accessioned2013-08-08T05:59:45Z-
dc.date.available2013-08-08T05:59:45Z-
dc.date.created2013-06-24-
dc.date.created2013-06-24-
dc.date.issued2013-06-
dc.identifier.citationAPPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, v.170, no.4, pp.787 - 804-
dc.identifier.issn0273-2289-
dc.identifier.urihttp://hdl.handle.net/10203/174715-
dc.description.abstractFor bacterial cell surface display, the target protein needs to be linked to an anchoring motif, and it is essential to choose an appropriate anchoring motif for efficient and stable display of the protein on the cell surface. To isolate a potential anchoring motif that would allow a stable and enhanced display of target proteins on the surface of an Escherichia coli host, we analyzed the outer membrane proteome of E. coli. On the basis of this proteomic analysis, the outer membrane protein X (OmpX), which has a small, monomeric beta-barrel structure and is highly expressed, was selected as a potential anchoring motif. The role of OmpX as an anchoring motif for cell surface display was demonstrated using three important industrial enzymes: endoxylanase, lipase, and alkaline phosphatase. Two different positions (Lys(122), Val(160)) in the extracellular loops of OmpX were examined for C-terminal fusion, and the biological activities and localization of the displayed enzymes were analyzed. All three enzymes examined were efficiently displayed on the E. coli cell surface with high activity. These results reveal that the use of OmpX as an anchoring motif is an efficient method to display functional enzymes on the surface of an E. coli host.-
dc.languageEnglish-
dc.publisherHUMANA PRESS INC-
dc.subjectOUTER-MEMBRANE-
dc.subjectBETA-BARREL-
dc.subjectPROTEINS-
dc.subjectLIPASE-
dc.subjectIDENTIFICATION-
dc.subjectPEPTIDES-
dc.subjectYEAST-
dc.subjectOMPX-
dc.titleIsolation of a Potential Anchoring Motif Based on Proteome Analysis of Escherichia coli and Its Use for Cell Surface Display-
dc.typeArticle-
dc.identifier.wosid000319161000004-
dc.identifier.scopusid2-s2.0-84878219023-
dc.type.rimsART-
dc.citation.volume170-
dc.citation.issue4-
dc.citation.beginningpage787-
dc.citation.endingpage804-
dc.citation.publicationnameAPPLIED BIOCHEMISTRY AND BIOTECHNOLOGY-
dc.identifier.doi10.1007/s12010-013-0236-9-
dc.contributor.localauthorJeong, Kijun-
dc.contributor.nonIdAuthorYim, Sung Sun-
dc.contributor.nonIdAuthorAn, Seul Ji-
dc.contributor.nonIdAuthorHan, Mee-Jung-
dc.contributor.nonIdAuthorChoi, Jae Woong-
dc.type.journalArticleArticle-
dc.subject.keywordAuthorCell surface display-
dc.subject.keywordAuthorProteome-
dc.subject.keywordAuthorOuter membrane protein X-
dc.subject.keywordAuthorEscherichia coli-
dc.subject.keywordPlusOUTER-MEMBRANE-
dc.subject.keywordPlusBETA-BARREL-
dc.subject.keywordPlusPROTEINS-
dc.subject.keywordPlusLIPASE-
dc.subject.keywordPlusIDENTIFICATION-
dc.subject.keywordPlusPEPTIDES-
dc.subject.keywordPlusYEAST-
dc.subject.keywordPlusOMPX-
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