The present study deals with the detailed investigation of the IgE antibody response of a gum arabic-allergic patient. The patient showed multiple serologic and skin test sensitizations to a range of pollen, other inhalants and foods, and bee venom, and to the recombinant allergens Bet v 1 and Bet v 2. Moreover, the patient's serum reacted strongly to gum-arabic extract. The NaIO4-treated and thus deglycosylated extract showed no binding to IgE. In contrast, removal of the protein backbone by basic hydrolysis did not deplete the IgE reactivity. Therefore, it is concluded that the gum arabic-specific IgE antibodies of this patient were mainly directed against the carbohydrate fraction of this material. In IgE-inhibition assays, cross-reactions occurred in the range of 60% between gum arabic and known immunogenic N-glycans containing α1-3-linked fucose. Since the inhibition graphs were not parallel and the inhibition was not complete with heterologue antigens, the cross-reacting epitopes of gum arabic appeared to be different from the latter well-known cross-reactive carbohydrate determinants (CCD). Inhibition may have been caused by a partial immunologic identity of the investigated carbohydrate moieties. A strong IgE response to the fucose-containing glycan from bromelain was measured in a glycan ELISA that utilizes purified glycopeptides at the solid phase. This response, which may explain the multiple sensitizations without clinical significance diagnosed in the patient, could originate from inhalation of pollen, which is known to contain similar glycans, or from occupational sensitization during work as a baker and confectioner. Since the gum-arabic protein showed only very weak participation in the IgE reactivity, the clinical symptoms of the patient caused by gum arabic may be attributed to carbohydrate epitopes. Due to the repetitive polysaccharide sequence of gum arabic, several epitopes for the cross-linking of IgE should exist.