Glycoengineering of the methylotrophic yeast Hansenula polymorpha for the production of glycoproteins with trimannosyl core N-glycan by blocking core oligosaccharide assembly.
DC Field | Value | Language |
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dc.contributor.author | Oh, Doo-Byoung | - |
dc.contributor.author | Park, Jeong-Seok | - |
dc.contributor.author | Kim, Moo Woong | - |
dc.contributor.author | Cheon, Seon Ah | - |
dc.contributor.author | Kim, Eun Jung | - |
dc.contributor.author | Moon, Hye Yun | - |
dc.contributor.author | Kwon, Ohsuk | - |
dc.contributor.author | Rhee, Sang Ki | - |
dc.contributor.author | Kang, Hyun Ah | - |
dc.date.accessioned | 2022-05-11T02:40:31Z | - |
dc.date.available | 2022-05-11T02:40:31Z | - |
dc.date.issued | 2008-05 | - |
dc.identifier.issn | 1860-6768 | - |
dc.identifier.issn | 1860-7314 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/57517 | - |
dc.description.abstract | The 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.format.extent | 10 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | Wiley - VCH Verlag GmbH & CO. KGaA | - |
dc.title | Glycoengineering of the methylotrophic yeast Hansenula polymorpha for the production of glycoproteins with trimannosyl core N-glycan by blocking core oligosaccharide assembly. | - |
dc.type | Article | - |
dc.identifier.doi | 10.1002/biot.200700252 | - |
dc.identifier.bibliographicCitation | Biotechnology Journal, v.3, no.5, pp 659 - 668 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.scopusid | 2-s2.0-44949101441 | - |
dc.citation.endPage | 668 | - |
dc.citation.number | 5 | - |
dc.citation.startPage | 659 | - |
dc.citation.title | Biotechnology Journal | - |
dc.citation.volume | 3 | - |
dc.publisher.location | 독일 | - |
dc.subject.keywordAuthor | ALG3 | - |
dc.subject.keywordAuthor | Glycoengineering | - |
dc.subject.keywordAuthor | Hansenula polymorpha | - |
dc.subject.keywordAuthor | Trimannosyl core N-glycan | - |
dc.description.journalRegisteredClass | scopus | - |
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