Further structural studies of the carbohydrate moiety of the allergen Ag-54 (Cla h II) from the mould Cladosporium herbarum.
The carbohydrate moiety of the glycoprotein allergen Ag-54, isolated from the mould Cladosporium herbarum, has been characterised partly, using acetolysis, methylation analysis, and n.m.r. spectroscopy. Ag-54 contained a highly branched galactoglucomannan and two branched mannogluco-oligosaccharide chains. The oligosaccharides contained terminal, (1----4)-, and (1----4,6)-linked alpha-Glc residues and terminal, (1----2)-, and some (1----3)-linked alpha-Man residues. The n.m.r. data indicated the galactoglucomannan to have a main chain made up of (1----6)-linked alpha-Man and (1----4)-linked alpha-Glc residues, with the latter attached to position 6 of alpha-Man residues. Oligosaccharides with (1----6)-linked beta-Galf and (1----2)-linked alpha-Man were attached to the main chain. Acetolysis of the galactoglucomannan yielded linear and branched oligosaccharides. The presence of (1----2,3)-linked alpha-Man residues indicated either that other than (1----6) linkages were present in the main chain or that there was 2,3-branching in the side chains.
Swärd-Nordmo
M
M
Department of Pharmacy, University of Oslo, Norway.
Paulsen
B S
BS
Wold
J K
JK
Wehler
T
T
Jansson
P E
PE
D000485:Allergens / Q000737:chemistry*; D000946:Antigens, Fungal / Q000737:chemistry; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002241:Carbohydrates / Q000737:chemistry; D002963:Cladosporium / Q000737:chemistry / Q000276:immunology*; D006023:Glycoproteins / Q000737:chemistry* / Q000276:immunology; D008745:Methylation; D008969:Molecular Sequence Data; D008970:Molecular Weight
D000485:Allergens; D000946:Antigens, Fungal; D002241:Carbohydrates; D006023:Glycoproteins