The Glycoprotein Allergen Ag-54 (C1a h II) from Cladosporium herbarum

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Abstract
The carbohydrate-protein linkage of the allergen Ag-54 in the mould Cladosporium herbarum was studied after alkaline-borohydride treatment of the glycoprotein. By incorporating tritium into the peptide-linked monosaccharide through the alkaline scission of the linkage, it was demonstrated that the highly branched galactomannan moiety of Ag-54 was linked to the protein through mannose. Threonine was identified as the carbohydrate-linked amino acid. In addition, a few glucose units were peptide-linked, but the corresponding amino acids were not identified. When deglycosylated with trifl·uoromethanesulfonic acid, Ag-54 retained only 5% of its allergenic activity as compared to the native Ag-54 when tested by rocket immunoelectrophoresis and autoradiography. Immunological identity between native and deglycosylated Ag-54 was observed. Deglycosylation also resulted in reduced stability towards denaturation by heat or urea.

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