Structures of the glycosylphosphatidylinositol membrane anchors from Aspergillus fumigatus membrane proteins

T Fontaine, Thierry Magnin, Angela Mehlert, Douglas Lamont, J P Latge, Michael A. J. Ferguson

    Research output: Contribution to journalArticlepeer-review

    67 Citations (Scopus)

    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 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: Manalpha1-3Manalpha1-2Manalpha1-2Manalpha1-6Manalpha1-4GlcN.

    Original languageEnglish
    Pages (from-to)169-177
    Number of pages9
    JournalGlycobiology
    Volume13
    Issue number3
    DOIs
    Publication statusPublished - Mar 2003

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