Morelle W, Bernard M, Debeaupuis JP, Buitrago M, Tabouret M, Latge JP Galactomannoproteins of Aspergillus fumigatus Eukaryotic Cell4(7) (2005)
1308-1316
Aspergillusfumigatus CBS 144-89
(previously named:Sartoryafumigata CBS 144-89, Aspergillusfumigates CBS 144-89, Neosartoryafumigata CBS 144-89)
(Ancestor NCBI TaxID 746128,
species name lookup)
The structure was elucidated in this paper NCBI PubMed ID:16002656 Publication DOI:10.1128/EC.4.7.1308-1316.2005 Journal NLM ID:101130731 Publisher: American Society for Microbiology Correspondence: jplatgepasteur.fr Institutions: Unité des Aspergillus, Institut Pasteur, Paris, France, Bio-Rad, Clinical Microbiology Division, Steenvoorde, France
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 Hex(5-13)HexNAc(2) oligosaccharides, the major molecular species corresponding to Hex(6-8)HexNAc(2). 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-β-1,5-galactofuran chain of galactomannan or with Aspergillus-infected patient sera.
Methods: GC-MS, GLC, methylation analysis, TFA hydrolysis, MALD-MS Comments, role: N-glycan moiety is composed of a mixture of Hex5-13HexNAc2; absolute D-configurations and pyranose ring sizes were assumed by CSDB staff