Allergy to deamidated gluten in patients tolerant to wheat: specific epitopes linked to deamidation

Autor: Manon Pietri, F. Battais, Marie Bodinier, Colette Larré, Chantal Brossard, F. Pineau, S. Triballeau, Denise-Anne Moneret-Vautrin, Evelyne Paty, Sandra Denery-Papini, T. Mothes
Přispěvatelé: Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de la Recherche Agronomique (INRA), Département Polluants et Santé, Institut national de recherche et de sécurité (Vandoeuvre lès Nancy) (INRS ( Vandoeuvre lès Nancy)), Institute for Laboratory Medicine, Otto Wagner Hospital Vienna, Service de Pneumologie et d'Allergologie Pédiatrique, CHU Necker - Enfants Malades [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Université de Lorraine (UL), Centre hospitalier Jean Monnet
Jazyk: angličtina
Rok vydání: 2012
Předmět:
Zdroj: Allergy
Allergy, Wiley, 2012, 67, pp.1023-1032. ⟨10.1111/j.1398-9995.2012.02860.x⟩
ISSN: 0105-4538
1398-9995
DOI: 10.1111/j.1398-9995.2012.02860.x⟩
Popis: 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 IgE-binding epitopes. Methods Sera were obtained from 15 patients allergic to DG and from nine patients allergic to wheat proteins (WP). IgE-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 IgE from patients allergic to WP, responses of patients allergic to DG were homogeneous. In ELISA, all the sera displayed IgE 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 IgE binding to deamidated gliadins or peptides of the type QPEEPFPE.
Databáze: OpenAIRE