Characterization of putative glycosylphosphatidylinositol-anchoring motifs for surface display in the methylotrophic yeast Hansenula polymorpha

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dc.contributor.authorS A Cheon-
dc.contributor.authorJinhee Jung-
dc.contributor.authorJ H Choo-
dc.contributor.authorDoo-Byoung Oh-
dc.contributor.authorH A Kang-
dc.date.accessioned2017-04-19T09:58:57Z-
dc.date.available2017-04-19T09:58:57Z-
dc.date.issued2014-
dc.identifier.issn01415492-
dc.identifier.uri10.1007/s10529-014-1582-6ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/12306-
dc.description.abstractBioinformatic analysis of the genome of the methylotrophic yeast Hansenula polymorpha revealed 39 putative glycosylphosphatidylinositol-anchored proteins (GPI-proteins). Notably, dibasic motifs in the proximal ω-site, that has been reported as a plasma membrane retention signal in Saccharomyces cerevisiae GPI-proteins, were not found in any of the predicted GPI-proteins of H. polymorpha. To evaluate the in silico prediction, C-terminal peptides of 40 amino acids derived from ten H. polymorpha GPI-proteins were fused to the Aspergillus saitoi α-1,2-mannosidase (msdS). Cell wall fraction analysis showed that nine of the ten msdS-GPI fusion proteins were mostly localized at the cell wall. Surface expression of functional msdS was further confirmed by in vitro enzyme activity assay and by glycan structure analysis of cell wall mannoproteins. The recombinant H. polymorpha strains expressing surface-displayed msdS have the potential as useful hosts to produce glycoproteins with decreased mannosylation. ⓒ 2014 Springer Science+Business Media Dordrecht.-
dc.publisherSpringer-
dc.titleCharacterization of putative glycosylphosphatidylinositol-anchoring motifs for surface display in the methylotrophic yeast Hansenula polymorpha-
dc.title.alternativeCharacterization of putative glycosylphosphatidylinositol-anchoring motifs for surface display in the methylotrophic yeast Hansenula polymorpha-
dc.typeArticle-
dc.citation.titleBiotechnology Letters-
dc.citation.number10-
dc.citation.endPage2094-
dc.citation.startPage2085-
dc.citation.volume36-
dc.contributor.affiliatedAuthorDoo-Byoung Oh-
dc.contributor.alternativeName전선아-
dc.contributor.alternativeName정진희-
dc.contributor.alternativeName추진호-
dc.contributor.alternativeName오두병-
dc.contributor.alternativeName강현아-
dc.identifier.bibliographicCitationBiotechnology Letters, vol. 36, no. 10, pp. 2085-2094-
dc.identifier.doi10.1007/s10529-014-1582-6-
dc.subject.keywordGlycan trimming-
dc.subject.keywordGlycosylphosphatidylinositol-anchored proteins-
dc.subject.keywordHansenula polymorpha-
dc.subject.keywordYeast surface display-
dc.subject.localGlycan trimming-
dc.subject.localGlycosylphosphatidylinositol-anchored proteins-
dc.subject.localHansenula polymorpha-
dc.subject.localYeast surface display-
dc.description.journalClassY-
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