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Eukaryotic Cell, July 2005, p. 1308-1316, Vol. 4, No. 7
1535-9778/05/$08.00+0 doi:10.1128/EC.4.7.1308-1316.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
M. Bernard,1
J.-P. Debeaupuis,1
M. Buitrago,1,
M. Tabouret,2 and
J.-P. Latgé1*
Unité des Aspergillus, Institut Pasteur, 25, rue du Docteur Roux, 75724 Paris Cedex 15,1 Bio-Rad, Clinical Microbiology Division, 59114 Steenvoorde, France2
Received 3 February 2005/ Accepted 18 May 2005
Galactofuranose-containing molecules have been repeatedly shown to be important antigens among human fungal pathogens, including Aspergillus fumigatus. Immunogenic galactofuran determinants have been poorly characterized chemically, however. We reported here the characterization of two glycoproteins of A. fumigatus with an N-glycan containing galactofuranose. These proteins are a phospholipase C and a phytase. Chemical characterization of the N-glycan indicates that it is a mixture of Hex5-13HexNAc2 oligosaccharides, the major molecular species corresponding to Hex6-8HexNAc2. The N-glycan contained one galactofuranose unit that was in a terminal nonreducing position attached to the 2 position of Man. This single terminal nonreducing galactofuranose is essential for the immunoreactivity of the N-glycans assessed either with a monoclonal antibody that recognizes a tetra-ß-1,5-galactofuran chain of galactomannan or with Aspergillus-infected patient sera.
Present address: Unité Mixte de Recherche CNRS/USTL 8576, Glycobiologie Structurale et Fonctionnelle, IFR 118, Université des Sciences et Technologies de Lille 1, 59655 Villeneuve d'Ascq Cedex, France.
Present address: Instituto Carlos III, Madrid, Spain.
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