Molecular and immunological characterization of wheat Serpin (Tri a 33)
2012
Mameri, Hamza | Denery-Papini, Sandra | Pietri, Manon, M. | Tranquet, Olivier | Larré, Colette | Drouet, Martine, M. | Paty, Evelyne, E. | Jonathan, Anne-Marie, A.-M. | Beaudouin, Etienne, E. | Moneret-Vautrin, Denise-Anne, D.-A. | Moreau, Thierry | Briozzo, Pierre, P. | Gaudin, Jean-Charles | Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA) ; Institut National de la Recherche Agronomique (INRA) | Institut Jean-Pierre Bourgin (IJPB) ; Institut National de la Recherche Agronomique (INRA)-AgroParisTech | Biodiversité et Biotechnologie Fongiques (BBF) ; Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE) | Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE) | Unite Allergol Gen & Pneumol ; Centre Hospitalier Universitaire d'Angers (CHU Angers) ; PRES Université Nantes Angers Le Mans (UNAM)-PRES Université Nantes Angers Le Mans (UNAM) | Serv Pneumol & Allergol Pediat ; Hôpital Necker - Enfants Malades [AP-HP] ; Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP) | Hôpital Cochin [AP-HP] ; Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP) | Centre Hospitalier Emile Durkheim [Epinal] (CH Epinal / CHED) | Pathol Resp Proteolyse & Aerosoltherapapie U1100 ; Institut National de la Santé et de la Recherche Médicale (INSERM) | French National Research Agency [ANR-08-ALIA-14 Predexpitope]
Scope Several wheat proteins are responsible for food and respiratory allergies. Due to their large polymorphism, the allergenic potential of a number of them has not yet been precisely established. The aim of this work was to perform a thorough assessment of serpin (Tri a 33) allergenicity. Methods and results Recombinant wheat Serpin-Z2B isoform (rSerpin-Z2B) was expressed in Escherichia coli. Synchrotron radiation circular dichroism data indicated that the recombinant serpin contains slightly more beta-strands than a-helix structures. IgE reactivity of sera from 103 patients with food allergy and 29 patients with Baker's asthma was evaluated using ELISA, a model of basophil activation and linear epitope mapping (Pepscan). Twenty percent of patients with food allergy to wheat and 31% of those with Baker's asthma displayed rSerpin-Z2B-specific IgE in ELISA. The protein was able to induce IgE-dependent basophil degranulation. The Pepscan experiment identified four regions involved in IgE binding to serpin. Heating the protein induced its irreversible denaturation and impaired IgE binding, revealing the predominance of conformational epitopes. Conclusion This study confirms wheat serpin allergenicity and shows that recombinant serpin may be a marker of a broad spectrum of sensitization to wheat proteins.
اظهر المزيد [+] اقل [-]الكلمات المفتاحية الخاصة بالمكنز الزراعي (أجروفوك)
المعلومات البيبليوغرافية
تم تزويد هذا السجل من قبل Institut national de la recherche agronomique