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Structural analysis of N-/O-glycans assembled on proteins in yeastsopen access

Authors
Thak, Eun JungKim, JunghoLee, Dong-JikKim, Jeong YoonKang, Hyun Ah
Issue Date
Jan-2018
Publisher
MICROBIOLOGICAL SOCIETY KOREA
Keywords
yeast; protein glycosylation; N-/O-glycans; structure analysis
Citation
JOURNAL OF MICROBIOLOGY, v.56, no.1, pp 11 - 23
Pages
13
Journal Title
JOURNAL OF MICROBIOLOGY
Volume
56
Number
1
Start Page
11
End Page
23
URI
https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/1361
DOI
10.1007/s12275-018-7468-x
ISSN
1225-8873
1976-3794
Abstract
Protein glycosylation, the most universal and diverse post-translational modification, can affect protein secretion, stability, and immunogenicity. The structures of glycans attached to proteins are quite diverse among different organisms and even within yeast species. In yeast, protein glycosylation plays key roles in the quality control of secretory proteins, and particularly in maintaining cell wall integrity. Moreover, in pathogenic yeasts, glycans assembled on cell-surface glycoproteins can mediate their interactions with host cells. Thus, a comprehensive understanding of protein glycosylation in various yeast species and defining glycan structure characteristics can provide useful information for their biotechnological and clinical implications. Yeast-specific glycans are a target for glyco-engineering; implementing human-type glycosylation pathways in yeast can aid the production of recombinant glycoproteins with therapeutic potential. The virulence-associated glycans of pathogenic yeasts could be exploited as novel targets for antifungal agents. Nowadays, several glycomics techniques facilitate the generation of species- and strain-specific glycome profiles and the delineation of modified glycan structures in mutant and engineered yeast cells. Here, we present the protocols employed in our laboratory to investigate the N- and O-glycan chains released from purified glycoproteins or cell wall mannoproteins in several yeast species.
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자연과학대학 (생명과학과)
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