Structures of the glycosylphosphatidylinositol membrane anchors from Aspergillus fumigatus membrane proteins
Open Access
- 30 October 2002
- journal article
- research article
- Published by Oxford University Press (OUP) in Glycobiology
- Vol. 13 (3) , 169-177
- https://doi.org/10.1093/glycob/cwg004
Abstract
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 C24:0 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.Keywords
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