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Galactomannoproteins of Aspergillus fumigatus

Galactomannoproteins of Aspergillus fumigatus 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-ß-1,5-galactofuran chain of galactomannan or with Aspergillus -infected patient sera. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Eukaryotic Cell American Society For Microbiology

Galactomannoproteins of Aspergillus fumigatus

Galactomannoproteins of Aspergillus fumigatus

Eukaryotic Cell , Volume 4 (7): 1308 – Jul 1, 2005

Abstract

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-ß-1,5-galactofuran chain of galactomannan or with Aspergillus -infected patient sera.

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References (42)

Publisher
American Society For Microbiology
Copyright
Copyright © 2005 by the American Society For Microbiology.
ISSN
1535-9778
eISSN
1535-9778
DOI
10.1128/EC.4.7.1308-1316.2005
Publisher site
See Article on Publisher Site

Abstract

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-ß-1,5-galactofuran chain of galactomannan or with Aspergillus -infected patient sera.

Journal

Eukaryotic CellAmerican Society For Microbiology

Published: Jul 1, 2005

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