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[PROTOCOL] Structural analysis of N-/O-glycans assembled on proteins in yeasts
Eun Jung Thak 1, Jungho Kim 1, Dong-Jik Lee 1, Jeong Yoon Kim 2, Hyun Ah Kang 1
Journal of Microbiology 2018;56(1):11-23.
DOI: https://doi.org/10.1007/s12275-018-7468-x
Published online: January 4, 2018
1Department of Life Science, Chung-Ang University, Seoul 06974, Republic of Korea, 2Department of Microbiology and Molecular Biology, Chungnam National University, Daejeon 34134, Republic of Korea1Department of Life Science, Chung-Ang University, Seoul 06974, Republic of Korea, 2Department of Microbiology and Molecular Biology, Chungnam National University, Daejeon 34134, Republic of Korea
Corresponding author:  Hyun Ah Kang , Tel: +82-2-820-5863, 
Received: 3 November 2017   • Revised: 2 December 2017   • Accepted: 3 December 2017
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Abstract

Protein glycosylation, the most universal and diverse posttranslational 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 virulenceassociated 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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    [PROTOCOL] Structural analysis of N-/O-glycans assembled on proteins in yeasts
    J. Microbiol. 2018;56(1):11-23.   Published online January 4, 2018
    DOI: https://doi.org/10.1007/s12275-018-7468-x
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