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Glycobiology Advance Access originally published online on October 30, 2002
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Glycobiology, 2003, Vol. 13, No. 3 169-177
© 2003 Oxford University Press

Structures of the glycosylphosphatidylinositol membrane anchors from Aspergillus fumigatus membrane proteins

Thierry Fontaine1,2, Thierry Magnin2, Angela Melhert3, Douglas Lamont3, Jean-paul Latgé2 and Michael A.J. Ferguson3

2 Unité Des Aspergillus, Institut Pasteur, 25 Rue Du Docteur Roux, 75724 Paris Cedex 15, France
3 Division of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee, Wellcome Trust Biocentre, Dow Street, Dundee DD1 5EH, United Kingdom

Received on May 30, 2002; revised on September 3, 2002; accepted on September 3, 2002

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: Man{alpha}1-3Man{alpha}1-2Man{alpha}1-2Man{alpha}1-6Man{alpha}1-4GlcN.

1 To whom correspondence should be addressed; e-mail: tfontain{at}pasteur.fr


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