Abstract
Celery roots were processed by microwave heating, cooking, drying, γ-irradiation, ultra high pressure treatment and high voltage impulse treatment. The immunochemical stabilities of the three known allergenic structures of celery were tested with sera from patients who were sensitised to celery. In addition, rabbit antisera were used to detect the allergens profilin and Api g 1 on celery immunoblots. The specificity and reactivity of IgE from the patients' sera were investigated by immunoblotting, by an enzyme allergosorbent test (EAST) and by dose-related IgE inhibition experiments. The results of all three methods agreed closely and indicated high antigenic and allergenic activity in native celery which was reduced by thermal processing. The heat-stability of the known celery allergens decreased in the following order: carbohydrate epitopes> profilin>Api g 1. In contrast, the allergenicity was only mildly reduced by non-thermal processing. The results obtained with human IgE were confirmed by an in vitro mediator-release assay that is based on rat basophil leukemia cells (RBL cells) which were passively sensitised with celery-specific murine IgE. With sera from mice that had been immunised with native celery, the native sample and non-thermal celery preparations elicited the strongest mediator release, whereas a weak response was obtained with samples from heat-processed celery. These results agreed closely with the data obtained in allergic patients whose IgE antibodies were directed against the major protein allergen Api g 1. Our results may be helpful in risk assessment and in selecting food preparations which can be consumed without symptoms by a subgroup of celery-allergic patients with a known sensitisation pattern. ©1997 SCI
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