Structural Basis of IgE Binding to alpha- and gamma-Gliadins: Contribution of Disulfide Bonds and Repetitive and Nonrepetitive Domains - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of Agricultural and Food Chemistry Année : 2015

Structural Basis of IgE Binding to alpha- and gamma-Gliadins: Contribution of Disulfide Bonds and Repetitive and Nonrepetitive Domains

Yann Gohon
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Frank Wien

Résumé

Wheat products cause IgE-mediated allergies. The present study aimed to decipher the molecular basis of alpha- and gamma-gliadin allergenicity. Gliadins and their domains, the repetitive N-terminal and the nonrepetitive C-terminal domains, were cloned and expressed in Escherichia coli. Their secondary structures and their IgE binding capacity were compared with those of natural proteins before and after reduction/alkylation. Allergenicity was evaluated with sera from patients who had wheat food allergy or baker's asthma: The secondary structures of natural and recombinant proteins were slightly different. Compared with natural gliadins, recombinant proteins retained IgE binding but with reduced reactivity. Reduction/alkylation decreased IgE binding for both natural and recombinant gliadins. Although more continuous epitopes were identified in the N-terminal domains, of alpha- and gamma-gliadins, both the N-terminal and C-terminal domains contributed to IgE binding. As for other Members of the prolamin: superfamily, disulfide bonds appear to be of high importance for IgE binding.
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Dates et versions

hal-01204207 , version 1 (23-09-2015)

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Citer

Hamza Mameri, Chantal Brossard, Jean-Charles Gaudin, Yann Gohon, Evelyne Paty, et al.. Structural Basis of IgE Binding to alpha- and gamma-Gliadins: Contribution of Disulfide Bonds and Repetitive and Nonrepetitive Domains. Journal of Agricultural and Food Chemistry, 2015, 63 (29), pp.6546 - 6554. ⟨10.1021/acs.jafc.5b01922⟩. ⟨hal-01204207⟩
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