Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
Associated disease: infection due to Aspergillus fumigatus [ICD11:
XN5Z7 
]
NCBI PubMed ID: 28369326Publication DOI: 10.1093/glycob/cwx028Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: oka
bio.sojo-u.ac.jp
Institutions: Department of Bioscience and Biotechnology, Faculty of Agriculture, Kyushu University, Fukuoka, Japan, Department of Applied Microbial Technology, Faculty of Biotechnology and Life Science, Sojo University, Ikeda, Japan, Department of Infection and Host Defense, Tohoku Medical and Pharmaceutical University, Komatsushima, Japan, Graduate School of Environmental and Life Science, Okayama University, Tsushimanaka, Japan, Department of Nanoscience, Faculty of Engineering, Sojo University, Ikeda, Japan, Department of Applied Biochemistry and Food Science, Saga University, Saga, Japan
Previously, we reported that GfsA is a novel galactofuranosyltransferase involved in the biosynthesis of O-glycan, the proper maintenance of fungal morphology, the formation of conidia and anti-fungal resistance in Aspergillus nidulans and A. fumigatus (Komachi Y et al., 2013. GfsA encodes a novel galactofuranosyltransferase involved in biosynthesis of galactofuranose antigen of O-glycan in Aspergillus nidulans and Aspergillus fumigatus. Mol. Microbiol. 90:1054-1073). In the present paper, to gain an in depth-understanding of the enzymatic functions of GfsA in A. fumigatus (AfGfsA), we established an in vitro assay to measure galactofuranosyltransferase activity using purified AfGfsA, UDP-α-d-galactofuranose as a sugar donor, and p-nitrophenyl-β-D-galactofuranoside as an acceptor substrate. LC/MS, 1H-NMR and methylation analyses of the enzymatic products of AfGfsA revealed that this protein has the ability to transfer galactofuranose to the C-5 position of the β-galactofuranose residue via a β-linkage. AfGfsA requires a divalent cation of manganese for maximal activity and consumes UDP-α-d-galactofuranose as a sugar donor. Its optimal pH range is 6.5-7.5 and its optimal temperature range is 20-30°C. 1H-NMR, 13C-NMR and methylation analyses of fungal-type galactomannan extracted from the ∆AfgfsA strain revealed that AfGfsA is responsible for the biosynthesis of β1,5-galactofuranose in the galactofuran side chain of fungal-type galactomannan. Based on these results, we conclude that AfGfsA acts as a UDP-α-d-galactofuranose: β-D-galactofuranoside β1,5-galactofuranosyltransferase in the biosynthetic pathway of galactomannans.
cell wall, galactofuranose, glycosyltransferase, Galactomannan, Aspergillus
Structure type: structural motif or average structure
Location inside paper: Fig. 6B
Compound class: galactomannan
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_136104,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141795,IEDB_141829,IEDB_141830,IEDB_141832,IEDB_141833,IEDB_143632,IEDB_144983,IEDB_149137,IEDB_149176,IEDB_152206,IEDB_153220,IEDB_164480,IEDB_190606,IEDB_76933,IEDB_885812,IEDB_983930,SB_136,SB_191,SB_196,SB_198,SB_44,SB_67,SB_72
Comments, role: representation of biosynthetic fungal-type galactomannan in Aspergillus fumigatus; absolute D-configurations and pyranose ring sizes of sugar residues were assumed by CSDB staff
Related record ID(s): 49013
NCBI Taxonomy refs (TaxIDs): 746128Reference(s) to other database(s): GTC:G03032WD
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There is only one chemically distinct structure:
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(previously named: Sartorya fumigata, Aspergillus fumigates, Neosartorya fumigata)