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Acid‐Hydrolyzed Gliadins Worsen Food Allergies through Early Sensitization
Author(s) -
Castan Laure,
Villemin Clélia,
Claude Mathilde,
Aubert Philippe,
Durand Tony,
Neunlist Michel,
Brossard Chantal,
Magnan Antoine,
Bodinier Marie,
Bouchaud Grégory
Publication year - 2018
Publication title -
molecular nutrition and food research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.495
H-Index - 131
eISSN - 1613-4133
pISSN - 1613-4125
DOI - 10.1002/mnfr.201800159
Subject(s) - deamidation , gliadin , sensitization , immune system , allergic response , allergy , food allergy , chemistry , intestinal permeability , immunology , antigen , gluten , biology , biochemistry , immunoglobulin e , antibody , enzyme
Scope Food allergies result from a complex immune response involving both innate and adaptive immune cells. Major proteins of wheat flour, gliadins, appear to be important allergens, and their characteristics can influence the allergic response. This study investigates the immune reaction when developing a food allergy to gliadins in native, deamidated, or hydrolyzed forms. Methods The immune response after one or two intraperitoneal sensitizations and after oral challenge with each gliadin form is analyzed. Results Results demonstrate that deamidated gliadins induce a stronger allergic reaction compared to native gliadins. Moreover, deamidation induces an earlier increase in intestinal permeability associated with more pronounced Th2 and Th17 polarizations together with an influx of antigen‐presenting cells, especially cDC2. Conclusion Altogether, Results indicate that industrial processes such as deamidation or hydrolysis influences food allergenicity through immune modulation and helps us to develop tools to determine how these processes can influence this reaction and encourage or decrease allergic reactions.