The glycoprotein allergen Ag-54 (Cla h II) from Cladosporium herbarum. Structural studies of the carbohydrate moiety.
The carbohydrate moiety of an important allergen, Ag-54 in Cladosporium herbarum was studied by alkaline-borohydride treatment, gel filtration, high-performance liquid chromatography, methylation analysis, gas liquid chromatography and mass spectometry. The Ag-54 protein core possessed a very limited number of sugar chains. The carbohydrate moiety consisted mainly of one large highly branched polysaccharide chain which accounted for nearly 75% of the total molecular weight of the glycoprotein. The carbohydrate moiety is made up of D-mannose and D-glucose units in pyranose form having D-galactofuranose side chains attached. Mannose is both 1,2- and 1,6-linked, while glucose is 1,4- and 1,6-linked. Some of the 1,6-linked galactofuranose side chains are bound through C-2 of the 1,6-linked mannose units, and the rest to C-3 of 1,6-linked mannose and 1,2-linked mannose units. A few oligoglucosidic chains of approximately 4 glucose units are also attached to the protein.
Swärd-Nordmo
M
M
Institute of Pharmacy, University of Oslo, Norway.
Paulsen
B S
BS
Wold
J K
JK
D000485:Allergens; D052179:Antigens, Plant; D002236:Carbohydrate Conformation; D002241:Carbohydrates / Q000032:analysis; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002963:Cladosporium / Q000276:immunology*; D005656:Fungal Proteins / Q000032:analysis*; D008745:Methylation; D003904:Mitosporic Fungi / Q000276:immunology*; D008970:Molecular Weight
D000485:Allergens; D052179:Antigens, Plant; D002241:Carbohydrates; C046933:Cla h II protein, Cladosporium herbarum; D005656:Fungal Proteins