Title |
[PROTOCOL] Structural analysis of N-/O-glycans assembled on proteins in yeasts |
Author |
Eun Jung Thak1, Jungho Kim1, Dong-Jik Lee1, Jeong Yoon Kim2, and Hyun Ah Kang1* |
Address |
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 Korea |
Bibliography |
Journal of Microbiology, 56(1),11–23, 2018,
|
DOI |
10.1007/s12275-018-7468-x
|
Key Words |
yeast, protein glycosylation, N-/O-glycans, structure analysis |
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. |