Characterization of N-linked oligosaccharides assembled on secretory recombinant glucose oxidase and cell wall mannoproteins from the methylotrophic yeast Hansenula ploymorpha

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Title
Characterization of N-linked oligosaccharides assembled on secretory recombinant glucose oxidase and cell wall mannoproteins from the methylotrophic yeast Hansenula ploymorpha
Author(s)
Moo Woong Kim; Sang Ki Rhee; J Y Kim; Y Shimma; Y Chiba; Y Jigami; Hyun Ah Kang
Bibliographic Citation
Glycobiology, vol. 14, no. 3, pp. 243-251
Publication Year
2004
Abstract
Presently almost no information is available on the oligosaccharide structure of the glycoproteins secreted from the methylotrophic yeast Hansenula polymorpha, a promising host for the production of recombinant proteins. In this study, we analyze the size distribution and structure of N-linked oligosaccharides attached to the recombinant glycoprotein glucose oxidase (GOD) and the cell wall manno-proteins obtained from H. polymorpha. Oligosaccharide profiling showed that the major oligosaccharide species derived from the H. polymorpha-secreted recombinant GOD (rGOD) had core-type structures (Man8-12GlcNAc2. Analyses using anti-α1,3-mannose antibody and exoglycosidases specific for α1,2- or ,6-mannose linkages revealed that the mannose outer chains of N-glycans on the rGOD have very short α1,6 extensions and are mainly elongated in α1,2-linkages without a terminal α1,3-linked mannose addition. The N-glycans released from the H. polymorpha mannoproteins were shown to contain mostly mannose in their outer chains, which displayed almost identical size distribution and structure to those of H. polymorpha-derived rGOD. These results strongly indicate that the outer chain processing of N-glycans by H. polymorpha significantly differs from that by Saccharomyces cerevisiae, thus generating much shorter mannose outer chains devoid of terminal α1,3-linked mannoses.
Keyword
Glycan profilingHansenula polymorphaN-linked oligosaccharidesRecombinant glucose oxidaseCell wall mannoproteins
ISSN
0959-6658
Publisher
Oxford Univ Press
DOI
http://dx.doi.org/10.1093/glycob/cwh030
Type
Article
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1. Journal Articles > Journal Articles
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