Glycoengineering of the methylotrophic yeast Hansenula polymorpha for the production of glycoproteins with trimannosyl core N-glycan by blocking core oligosaccharide assembly

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dc.contributor.authorDoo-Byoung Oh-
dc.contributor.authorJ S Park-
dc.contributor.authorMoo Woong Kim-
dc.contributor.authorSeon Ah Cheon-
dc.contributor.authorEun Jung Kim-
dc.contributor.authorHye Yun Moon-
dc.contributor.authorOh Suk Kwon-
dc.contributor.authorSang Ki Rhee-
dc.contributor.authorHyun Ah Kang-
dc.date.accessioned2017-04-19T09:11:04Z-
dc.date.available2017-04-19T09:11:04Z-
dc.date.issued2008-
dc.identifier.issn1860-6768-
dc.identifier.uri10.1002/biot.200700252ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/8487-
dc.description.abstractThe initial lipid-linked oligosaccharide Glc3Man9GlcNAc2-dolichyl pyrophosphate (Dol-PP) for N-glycan is synthesized and assembled at the membrane of the endoplasmic reticulum (ER) and subsequently transferred to a nascent polypeptide by the oligosaccharide transferase complex. We have identified an ALG3 homolog (HpALG3) coding for a dolichyl-phosphate-mannose dependent α-1,3-mannosyltransferase in the methylotrophic yeast Hansenula polymorpha. The detailed analysis of glycan structure by linkage-specific mannosidase digestion showed that HpALG3 is responsible for the conversion of MAn5GlcNAc2-Dol-PP to Man6GlcNAc2-Dol-PP, the first step to attach a mannose to the lipid-linked oligosaccharide in the ER. The N-glycosylation pathway of H. polymorpha has been remodeled by deleting the HpALG3 gene in the Hpoch1 null mutant strain blocked in the yeast-specific outer mannose chain synthesis and by introducing an ER-targeted Aspergillus saitoi α-1,2-mannosidase gene. This glycoengineered H. polymorpha strain produced glycoproteins mainly containing trimannosyl core N-glycan (Man3GlcNAc2), which is the common core backbone of various human-type N-glycans. The results demonstrate the high potential of H. polymorpha to be developed as an efficient expression system for the production of glycoproteins with humanized glycans.-
dc.publisherWiley-
dc.titleGlycoengineering of the methylotrophic yeast Hansenula polymorpha for the production of glycoproteins with trimannosyl core N-glycan by blocking core oligosaccharide assembly-
dc.title.alternativeGlycoengineering of the methylotrophic yeast Hansenula polymorpha for the production of glycoproteins with trimannosyl core N-glycan by blocking core oligosaccharide assembly-
dc.typeArticle-
dc.citation.titleBiotechnology Journal-
dc.citation.number5-
dc.citation.endPage668-
dc.citation.startPage659-
dc.citation.volume3-
dc.contributor.affiliatedAuthorDoo-Byoung Oh-
dc.contributor.affiliatedAuthorMoo Woong Kim-
dc.contributor.affiliatedAuthorSeon Ah Cheon-
dc.contributor.affiliatedAuthorEun Jung Kim-
dc.contributor.affiliatedAuthorHye Yun Moon-
dc.contributor.affiliatedAuthorOh Suk Kwon-
dc.contributor.affiliatedAuthorSang Ki Rhee-
dc.contributor.affiliatedAuthorHyun Ah Kang-
dc.contributor.alternativeName오두병-
dc.contributor.alternativeName박정석-
dc.contributor.alternativeName김무웅-
dc.contributor.alternativeName전선아-
dc.contributor.alternativeName김은중-
dc.contributor.alternativeName문혜연-
dc.contributor.alternativeName권오석-
dc.contributor.alternativeName이상기-
dc.contributor.alternativeName강현아-
dc.identifier.bibliographicCitationBiotechnology Journal, vol. 3, no. 5, pp. 659-668-
dc.identifier.doi10.1002/biot.200700252-
dc.subject.keywordALG3-
dc.subject.keywordGlycoengineering-
dc.subject.keywordHansenula polymorpha-
dc.subject.keywordTrimannosyl core N-glycan-
dc.subject.localALG3-
dc.subject.localGlyco-engineering-
dc.subject.localGlycoengineering-
dc.subject.localHansenulapolymorpha-
dc.subject.localhansenula polymorpha-
dc.subject.localHansenula polymorpha-
dc.subject.localHansenula polymorpha (Pichia angusta)-
dc.subject.localTrimannosyl core N-glycan-
dc.description.journalClassY-
Appears in Collections:
Aging Convergence Research Center > 1. Journal Articles
Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
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