Screening the allergenic repertoires of wheat and maize with sera from double-blind, placebo-controlled food challenge positive patients
Article first published online: 30 NOV 2005
Volume 61, Issue 1, pages 128–135, January 2006
How to Cite
Weichel, M., Vergoossen, N. J., Bonomi, S., Scibilia, J., Ortolani, C., Ballmer-Weber, B. K., Pastorello, E. A. and Crameri, R. (2006), Screening the allergenic repertoires of wheat and maize with sera from double-blind, placebo-controlled food challenge positive patients. Allergy, 61: 128–135. doi: 10.1111/j.1398-9995.2006.00999.x
- Issue published online: 30 NOV 2005
- Article first published online: 30 NOV 2005
- Accepted for publication 29 August 2005
- cDNA phage surface display;
- IgE-binding repertoires;
- maize allergy;
- recombinant allergens;
- wheat allergy
Background: Food allergy to wheat and maize is an increasing factor of deterioration of life quality, especially childhood and can, in rare cases, even induce anaphylaxis. Although omega-5 gliadin from wheat and maize lipid transfer protein have been characterized as major cereal allergens on the molecular level, the list of food allergens is far to be complete.
Methods: To identify the IgE-binding repertoires of wheat and maize we screened respective cDNA libraries displayed on phage surface with sera from patients with a confirmed food allergy. The study included six patients with a positive double-blind, placebo-controlled food challenge (DBPCFC) to wheat, nine patients with a positive DBPCFC to maize, and six patients with anaphylactic reactions after ingestion of wheat.
Results: The enriched sequences encoding IgE-binding proteins showed heterogeneous repertoires for both, wheat and maize. The selected wheat repertoire yielded 12, the maize repertoire 11 open reading frames. Among these we identified allergens belonging to already characterized allergens families, such as gliadin, profilin and beta-expansin. Besides, we found novel proteins with high cross-reactive potential, such as thioredoxins, as well as sequences that had so far not been related to cereal allergy at all. The IgE-binding capacity of some selected proteins was evaluated in vitro and cross-reactivity was demonstrated by competition ELISA.
Conclusion: With regard to the heterogeneity of the characterized sequences as well as to the biochemical nature of the new allergens detected we conclude that wheat and maize-related food allergy is more complex than so far anticipated.