학술논문

Anaphylaxis to camomile: clinical features and allergen cross-reactivity
Document Type
Academic Journal
Source
Clinical & Experimental Allergy. Oct 01, 2000 30(10):1436-1443
Subject
Language
English
ISSN
0954-7894
Abstract
BACKGROUND: Medicinal remedies of plant origin became very popular in recent years, and allergic reactions to these are on the rise, accordingly. Camomile has been reported as a potential trigger of severe anaphylaxis. The allergens responsible for camomile allergy have not been characterized as yet. OBJECTIVE: The present study aims at reviewing the clinical symptomatology of immediate-type reactions in a series of patients sensitized to camomile and at characterizing the responsible allergens. METHODS: Fourteen patients with a history of allergy either to camomile or to spices or weeds, and a positive skin prick test/RAST to camomile were investigated for related allergic reactions to food, pollen and others. IgE-binding patterns were determined by immunoblotting, inhibition tests and deglycosylation experiments. RESULTS: Ten of 14 patients had a clinical history of immediate-type reactions to camomile, in some cases life threatening. Eleven subjects were also sensitized to mugwort in prick or RAST, eight to birch tree pollen. Using a polyclonal rabbit anti-Bet v 1 antibody, a homologue of the major birch pollen allergen Bet v 1 was detected in two camomile blots. In four cases a group of higher molecular weight allergens (23–50 kDa) showed IgE-binding to camomile. All allergens proved heat stable. Binding was inhibited in variable degrees by extracts from celery roots, anize seeds and pollen from mugwort, birch and timothy grass. Deglycosylation experiments proved the presence of carbohydrate determinants in camomile which were not responsible for IgE-binding, though. Profilins (Bet v 2) were not detected in our camomile extracts. CONCLUSION: Incidence and risk of type I allergy to camomile may be underestimated. Concurrent sensitization to mugwort and birch pollen is not infrequent. Bet v 1 and noncarbohydrate higher molecular weight proteins were found to be eliciting allergens and are responsible for cross-reactivity with other foods and pollen.