Immunoglobulin-E-binding epitopes of wheat allergens in patients with food allergy to wheat and in mice experimentally sensitized to wheat proteins
Autor: | K. Adel-Patient, Didier Marion, Bénédicte Bakan, Denise-Anne Moneret-Vautrin, Sandra Denery-Papini, F. Pineau, Marie Bodinier, D. Kasarda, T. Mothes, Hamza Mameri, S. Triballeau, Olivier Tranquet |
---|---|
Rok vydání: | 2011 |
Předmět: |
0303 health sciences
Allergy biology Immunology food and beverages medicine.disease Immunoglobulin E medicine.disease_cause Epitope 03 medical and health sciences 0302 clinical medicine Epitope mapping 030228 respiratory system Antigen Pepscan Food allergy Allergic response medicine biology.protein Immunology and Allergy 030304 developmental biology |
Zdroj: | Clinical & Experimental Allergy. 41:1478-1492 |
ISSN: | 0954-7894 |
DOI: | 10.1111/j.1365-2222.2011.03808.x |
Popis: | Summary Background At present, B cell epitopes involved in food allergy to wheat are known only for a few allergens and a few categories of patients. Objective To characterize the epitopes of different wheat kernel allergens: α-, γ, ω2, and ω5-gliadin, a low-molecular-weight (LMW) glutenin subunit, and a lipid transfer protein (LTP1) recognized by allergic patients and by sensitized mice and provide further understanding of the role of structure in determining allergic response. Methods Sera were obtained from 39 patients suffering from food allergy to wheat. BALB/c mice were sensitized to gliadins or LTP1 by intraperitoneal immunizations. Continuous epitopes bound by IgE were delineated by the Pepscan technique. The response to reduced, alkylated LTP1 was compared with that of the native form to evaluate the importance of protein folding on IgE reactivity. Results Few continuous epitopes of LTP1 reacted with IgE from allergic patients and mice, but one of them was common to several patients and sensitized mice. The unfolded protein was not recognized by either patient or mouse IgE, emphasizing the major role of LTP1 folding and discontinuous epitopes in IgE-binding. In contrast, many continuous epitopes were detected by patient and mouse IgE especially for an ω5-gliadin, which is an unstructured protein, and to a lesser extent, for the other gliadins and a LMW-glutenin subunit. Conclusion and Clinical Relevance The conformation of LTP1 appeared to have a strong impact on the type of IgE-binding epitopes elicited by this protein in both man and mouse. The responses in mice sensitized to gliadins or LTP1 were sufficiently comparable with the human response in terms of IgE-binding epitopes to provide support for the use of the mouse model in further investigations. Cite this as: S. Denery-Papini, M. Bodinier, F. Pineau, S. Triballeau, O. Tranquet, K. Adel-Patient, D.A. Moneret-Vautrin, B. Bakan, D. Marion, T. Mothes, H. Mameri and D. Kasarda, Clinical & Experimental Allergy, 2011 (41) 1478–1492. |
Databáze: | OpenAIRE |
Externí odkaz: |