The structure was elucidated in this paper Publication DOI:10.1093/glycob/cwg004 Journal NLM ID:9104124 Publisher: IRL Press at Oxford University Press Correspondence: Thierry Fontaine <tfontainpasteur.fr> Institutions: Unité Des Aspergillus, Institut Pasteur, 25 Rue Du Docteur Roux, 75724 Paris Cedex 15, France, Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Wellcome Trust Biocentre, Dow Street, Dundee DD1 5EH, United Kingdom
Glycosylphosphatidylinositol (GPI)-anchored proteins have been identified in all eukaryotes. In fungi, structural and biosynthetic studies of GPIs have been restricted to the yeast Saccharomyces cerevisiae. In this article, four GPI-anchored proteins were purified from a membrane preparation of the human filamentous fungal pathogen Aspergillus fumigatus. Using new methodology applied to western blot protein bands, the GPI structures were characterized by ES-MS, fluorescence labeling, HPLC, and specific enzymatic digestions. The phosphatidylinositol moiety of the A. fumigatus GPI membrane anchors was shown to be an inositol-phosphoceramide containing mainly phytosphingosine and monohydroxylated C-24:0 fatty acid. In constrast to yeast, only ceramide was found in the GPI anchor structures of A. fumigatus, even for Gel1p, a homolog of Gas1p in S. cerevisiae that contains diacylglycerol. The A. fumigatus GPI glycan moiety is mainly a linear pentomannose structure linked to a glucosamine residue: Manα1-3Manα1-2Manα1-2Manα1-6Manα1-4GlcN.
Methods: SDS-PAGE, sugar analysis, TLC, ESI-MS, Western blotting, MALDI-TOF MS, HPLC, enzymatic digestion, HF treatment, permethylation Comments, role: The position of phosphoethanolamine linked to the protein is suggested by studies in other eukaroytes.
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