Cry j I, a major allergenic glycoprotein of Cryptomeria japonica (Japanese cedar, Sugi), is the most commom pollen allergen in Japan. Carbohydrate analysis and lectin staining indicated that Cry j I possesses the fucose/xylose-containing N-linked oligosaccharide which previously has been found in some plant glycoproteins. Rabbit polyclonal anti-Cry j I IgG antibodies were found to be highly cross-reactive with two other plant glycoproteins which have the same type of oligosaccharides, and the cross-reactivities were completely abolished on chemical deglycosylation of the glycoproteins. Enzyme-linked immunosorbent assay inhibition showed that the majority (up to 70%) of the anti-Cry j I rabbit IgG antibodies recognized the oligosaccharide moiety of Cry j I. The carbohydrate epitopes were found to be only partially involved in the binding of specific IgE antibodies from a pool of human patient sera.

Keywords:
Carbohydrate, Cry j I, antigenicity, Epitope, Oligosaccharide, Pollen allergen
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© 1994 S. Karger AG, Basel
1994
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