Structural Basis of IgE Binding to α- and γ-Gliadins: Contribution of Disulfide Bonds and Repetitive and Nonrepetitive Domains-Reference-Cited by-同舟云学术

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

Published:2015-07-17 Issue:29 Volume:63 Page:6546-6554
ISSN:0021-8561
Container-title:Journal of Agricultural and Food Chemistry
language:en
Short-container-title:J. Agric. Food Chem.

Author:

Mameri Hamza¹²,Brossard Chantal¹,Gaudin Jean-Charles¹,Gohon Yann²,Paty Evelyne³,Beaudouin Etienne⁴,Moneret-Vautrin Denise-Anne⁴,Drouet Martine⁵,Solé Véronique¹,Wien Frank⁶,Lupi Roberta¹,Larré Colette¹,Snégaroff Jacques²,Denery-Papini Sandra¹

Affiliation:

1. INRA, UR1268 BIA (Biopolymers, Interactions, Assemblies), F-44316 Nantes, France

2. INRA, UMR1318, Institut Jean-Pierre Bourgin, INRA-AgroParisTech, F-78026 Versailles, France

3. Service de Pneumologie et d’Allergologie Pédiatrique, Groupe hospitalier Necker, F-75015 Paris, France

4. Service d’Allergologie, CH Epinal, F-88021 Epinal, France

5. Unité d’Allergologie Générale et de Pneumologie, CHU d’Angers, F-49933 Angers, France

6. Synchrotron Soleil, Saint-Aubin, F-91192 Gif-sur-Yvette, France

Funder

Agence Nationale de la Recherche

Publisher

American Chemical Society (ACS)

Subject

General Agricultural and Biological Sciences,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jafc.5b01922

Reference43 articles.

1. Evolutionary biology of plant food allergens

2. Allergens are distributed into few protein families and possess a restricted number of biochemical functions

3. The conformation of wheat gluten proteins. The secondary structures and thermal stabilities of α-, β-, γ- and ω-Gliadins

4. Immunoglobulin-E-binding epitopes of wheat allergens in patients with food allergy to wheat and in mice experimentally sensitized to wheat proteins

5. Trypsin resistance of the major peanut allergen Ara h 6 and allergenicity of the digestion products are abolished after selective disruption of disulfide bonds

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