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Glycobiology Advance Access published online on December 23, 2003
Glycobiology, doi:10.1093/glycob/cwh030
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Submitted on August 27, 2003
Revised on October 27, 2003
Accepted on October 30, 2003

© 2003 Oxford University Press

ORIGINAL ARTICLES

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

Moo Woong Kim 1, Sang Ki Rhee 2, Jeong-Yoon Kim 3, Yoh-ichi Shimma 4, Yasunori Chiba 4, Yoshifumi Jigami 4, and Hyun Ah Kang 2*

1 Metabolic Engineering Laboratory, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-600, Korea; Department of Microbiology, Chungnam National University, Daejeon 305-764, Korea
2 Metabolic Engineering Laboratory, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-600, Korea
3 Department of Microbiology, Chungnam National University, Daejeon 305-764, Korea
4 Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology (AIST), 1-1-4 Higashi, Tsukuba, Ibaraki, 305-8566, Japan

* To whom correspondence should be addressed. E-mail: hyunkang{at}mail.kribb.re.kr.

Abstract

At present, 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 analyzed the size distribution and structure of N-linked oligosaccharides attached to the recombinant glycoprotein glucose oxidase (GOD) and the cell wall mannoproteins 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-{alpha}1,3-mannose antibody and exoglycosidases specific for {alpha}1,2- or {alpha}1,6-mannose linkages revealed that the mannose outer chains of N-glycans on the rGOD have very short {alpha}1,6 extensions and are mainly elongated in {alpha}1,2-linkages without terminal {alpha}1,3-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 {alpha}1,3-linked mannoses.


Cell wall mannoproteins, Glycan profiling, Hansenula polymorpha, N-linked oligosaccharides, Recombinant glucose oxidase
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