Acid Hydrolysis of Gluten Enhances the Skin Sensitizing Potential and Drives Diversification of IgE Reactivity to Unmodified Gluten Proteins.

Brown Norway rats deamidation hydrolysis skin sensitization wheat allergy

Journal

Molecular nutrition & food research
ISSN: 1613-4133
Titre abrégé: Mol Nutr Food Res
Pays: Germany
ID NLM: 101231818

Informations de publication

Date de publication:
12 2021
Historique:
revised: 23 09 2021
received: 02 05 2021
pubmed: 13 10 2021
medline: 1 4 2022
entrez: 12 10 2021
Statut: ppublish

Résumé

Personal care products containing hydrolyzed gluten have been linked to spontaneous sensitization through the skin, however the impact of the hydrolysate characteristics on the sensitizing capacity is generally unknown. The physicochemical properties of five different wheat-derived gluten products (one unmodified, one enzyme hydrolyzed, and three acid hydrolyzed) are investigated, and the skin sensitizing capacity is determined in allergy-prone Brown Norway rats. Acid hydrolyzed gluten products exhibited the strongest intrinsic sensitizing capacity via the skin. All hydrolyzed gluten products induced cross-reactivity to unmodified gluten in the absence of oral tolerance to wheat, but were unable to break tolerance in animals on a wheat-containing diet. Still, the degree of deamidation in acid hydrolyzed products is associated with product-specific sensitization in wheat tolerant rats. Sensitization to acid hydrolyzed gluten products is associated with a more diverse IgE reactivity profile to unmodified gluten proteins compared to sensitization induced by unmodified gluten or enzyme hydrolyzed gluten. Acid hydrolysis enhances the skin sensitizing capacity of gluten and drives IgE reactivity to more gluten proteins. This property of acid hydrolyzed gluten may be related to the degree of product deamidation, and could be a strong trigger of wheat allergy in susceptible individuals.

Identifiants

pubmed: 34636481
doi: 10.1002/mnfr.202100416
doi:

Substances chimiques

Allergens 0
Immunoglobulin E 37341-29-0
Glutens 8002-80-0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

e2100416

Informations de copyright

© 2021 Wiley-VCH GmbH.

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Auteurs

Anne-Sofie Ravn Ballegaard (AR)

National Food Institute, Technical University of Denmark, Kgs. Lyngby, 2800, Denmark.

Laure Castan (L)

INRAE BIA UR1268, Nantes, 44316, France.
Institut du thorax, INSERM CNRS, UNIV Nantes, Nantes, 44000, France.

Jeppe Madura Larsen (JM)

National Food Institute, Technical University of Denmark, Kgs. Lyngby, 2800, Denmark.

Cristian Piras (C)

Department of Health Sciences, University Magna Graecia of Catanzaro, Catanzaro, 88100, Italy.

Clélia Villemin (C)

INRAE BIA UR1268, Nantes, 44316, France.

Daniel Andersen (D)

Department of Biotechnology and Biomedicine, Technical University of Denmark, Kgs. Lyngby, 2800, Denmark.

Charlotte Bernhard Madsen (CB)

National Food Institute, Technical University of Denmark, Kgs. Lyngby, 2800, Denmark.

Paola Roncada (P)

Department of Health Sciences, University Magna Graecia of Catanzaro, Catanzaro, 88100, Italy.

Susanne Brix (S)

Department of Biotechnology and Biomedicine, Technical University of Denmark, Kgs. Lyngby, 2800, Denmark.

Sandra Denery-Papini (S)

INRAE BIA UR1268, Nantes, 44316, France.

Gabriel Mazzucchelli (G)

Laboratory of Mass Spectrometry - MolSys, Department of Chemistry, University of Liege, Liege, 4000, Belgium.
GIGA Proteomics Facility, University of Liege, Liege, 4000, Belgium.

Grégory Bouchaud (G)

INRAE BIA UR1268, Nantes, 44316, France.

Katrine Lindholm Bøgh (KL)

National Food Institute, Technical University of Denmark, Kgs. Lyngby, 2800, Denmark.

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