期刊
FUNGAL GENETICS AND BIOLOGY
卷 56, 期 -, 页码 107-115出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.fgb.2013.03.009
关键词
Candida albicans; Glycosylation; Cell wall; Glycosylation reporter
资金
- Wellcome Trust [080088]
- BBSRC [BB/F00513X/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/F00513X/1] Funding Source: researchfish
A large proportion of Candida albicans cell surface proteins are decorated post-translationally by glycosylation. Indeed N-glycosylation is critical for cell wall biogenesis in this major fungal pathogen and for its interactions with host cells. A detailed understanding of N-glycosylation will yield deeper insights into host-pathogen interactions. However, the analysis of N-glycosylation is extremely challenging because of the complexity and heterogeneity of these structures. Therefore, in an attempt to reduce this complexity and facilitate the analysis of N-glycosylation, we have developed new synthetic C. albicans reporters that carry a single N-linked glycosylation site derived from Saccharomyces cerevisiae Suc2. These glycosylation reporters, which carry C albicans Hex1 or Sap2 signal sequences plus carboxy-terminal FLAG(3) and His(6) tags, were expressed in C. albicans from the ACT1 promoter. The reporter proteins were successfully secreted and hyperglycosylated by C albicans cells, and their outer chain glycosylation was dependent on Och1 and Pmr1, which are required for N-mannan synthesis, but not on Mnt1 and Mnt2 which are only required for O-mannosylation. These reporters are useful tools for the experimental dissection of N-glycosylation and other related processes in C. albicans, such as secretion. (C) 2013 The Authors. Published by Elsevier Inc. All rights reserved.
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