Engineering of the yeast Yarrowia lipolytica for the production of glycoproteins lacking the outer-chain mannose residues of N-glycansopen access
- Authors
- Song, Yunkyoung; Choi, Min Hee; Park, Jeong-Nam; Kim, Moo Woong; Kim, Eun Jung; Kang, Hyun Ah; Kim, Jeong-Yoon
- Issue Date
- Jul-2007
- Publisher
- AMER SOC MICROBIOLOGY
- Citation
- APPLIED AND ENVIRONMENTAL MICROBIOLOGY, v.73, no.14, pp 4446 - 4454
- Pages
- 9
- Journal Title
- APPLIED AND ENVIRONMENTAL MICROBIOLOGY
- Volume
- 73
- Number
- 14
- Start Page
- 4446
- End Page
- 4454
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/56994
- DOI
- 10.1128/AEM.02058-06
- ISSN
- 0099-2240
1098-5336
- Abstract
- In an attempt to engineer a Yarrowia lipolytica strain to produce glycoproteins lacking the outer-chain mannose residues of N-linked oligosaccharides, we investigated the functions of the OCH1 gene encoding a putative alpha-1,6-mannosyltransferase in Y. lipolytica. The complementation of the Saccharomyces cerevisiae och1 mutation by the expression of YlOCH1 and the lack of in vitro alpha-1,6-mannosyltransferase activity in the Yloch1 null mutant indicated that Yl0CH1 is a functional ortholog of S. cerevisiae OCH1. The oligosaccharides assembled on two secretory glycoproteins, the Trichoderma reesei endoglucanase I and the endogenous Y. lipolytica lipase, from the Yloch1 null mutant contained a single predominant species, the core oligosaccharide Man(8)GlcNAc(2), whereas those from the wild-type strain consisted of oligosaccharides with heterogeneous sizes, Man(8)GlcNAc(2) to Man(12)GlcNAc(2). Digestion with alpha-1,2- and alpha-1,6-mannosidase of the oligosaccharides from the wild-type and Yloch1 mutant strains strongly supported the possibility that the Yloch1 mutant strain has a defect in adding the first alpha-1,6-linked mannose to the core oligosaccharide. Taken together, these results indicate that YlOCH1 plays a key role in the outer-chain mannosylation of N-linked oligosaccharides in Y. lipolytica. Therefore, the Yloch1 mutant strain can be used as a host to produce glycoproteins lacking the outer-chain mannoses and further developed for the production of therapeutic glycoproteins containing human-compatible oligosaccharides.
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