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Background Gluten proteins can be modified by deamidation to enhance their solubility and technological applications. However, severe allergic reactions have been reported after the consumption of food products containing deamidated gluten ( DG) in subjects tolerant to wheat. This work aimed to characterize allergen profiles for these patients in comparison with those of patients allergic to wheat and to identify Ig E-binding epitopes. Methods Sera were obtained from 15 patients allergic to DG and from nine patients allergic to wheat proteins ( WP). Ig E-binding profiles were characterized both in ELISA and in a humanized rat basophilic leukaemia ( RBL) cell model. Epitopes were mapped on γ- and ω2-gliadin sequences by Pepscan, and effect of glutamine/glutamic acid substitutions was studied. Results Compared to the heterogeneous pattern of allergens detected by Ig E from patients allergic to WP, responses of patients allergic to DG were homogeneous. In ELISA, all the sera displayed Ig E binding to deamidated γ- and ω2-gliadins and deamidated total gliadins, frequently with high concentrations. These modified proteins induced RBL degranulation with most of the sera from DG-allergic patients. A consensus epitope was found on native γ- and ω2-gliadins ( QPQQPFPQ); it was repeated several times in their sequences. The substitution of two or three glutamines of this epitope into glutamic acid at positions Q3 or Q4 and Q8 ( QPEEPFPE) increased its recognition the best. Conclusion Allergy to DG is a separate entity from wheat allergy. It can be evidenced by strong Ig E binding to deamidated gliadins or peptides of the type QPEEPFPE. [ABSTRACT FROM AUTHOR]

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. [ABSTRACT FROM AUTHOR]