Structural analysis of N-/O-glycans assembled on proteins in yeastsopen access
- Authors
- Thak, Eun Jung; Kim, Jungho; Lee, Dong-Jik; Kim, Jeong Yoon; Kang, 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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