title: The thermal aggregation of ovalbumin as large particles decreases its allergenicity for egg allergic patients and in a murine model.
abstract: Most egg-allergic children can tolerate extensively cooked eggs. Ovalbumin, a major allergen in egg whites, is prone to aggregate upon heating. This study compares ovalbumin's allergenicity when it is aggregated as large particles to ovalbumin in its native form. Immunoglobulins (Ig)-binding and the degranulation capacities of native and aggregated ovalbumin were measured with sera from egg-allergic children and from mice sensitized to native or aggregated ovalbumin. The influence of ovalbumin structure on Ig production upon sensitization and elicitation potency by challenge was also studied. We showed that heat aggregation of ovalbumin as large particles enhances IgG production and promotes IgG2a production (a shift toward the T helper 1 profile). Aggregated ovalbumin displayed lower Ig-binding and basophil-activation capacities for sera from both allergic patients and mice. This work illustrates the links between ovalbumin structure after heating and allergenicity potential using parameters from both the sensitization and elicitation phases of the allergic reaction.
authors.affiliation: INRA, UR 1268 BIA (Biopolymers, Interactions, Assemblies), F-44316, rue de la Géraudière, 44316 Nantes, France.
authors.forename: M
authors.initials: M
authors.lastname: Claude
authors.affiliation: INRA, UR 1268 BIA (Biopolymers, Interactions, Assemblies), F-44316, rue de la Géraudière, 44316 Nantes, France.
authors.forename: R
authors.initials: R
authors.lastname: Lupi
authors.affiliation: INRA, UR 1268 BIA (Biopolymers, Interactions, Assemblies), F-44316, rue de la Géraudière, 44316 Nantes, France.
authors.forename: G
authors.initials: G
authors.lastname: Bouchaud
authors.affiliation: INRA, UR 1268 BIA (Biopolymers, Interactions, Assemblies), F-44316, rue de la Géraudière, 44316 Nantes, France.
authors.forename: M
authors.initials: M
authors.lastname: Bodinier
authors.affiliation: INRA, UR 1268 BIA (Biopolymers, Interactions, Assemblies), F-44316, rue de la Géraudière, 44316 Nantes, France. Electronic address: chantal.brossard@nantes.inra.fr.
authors.forename: C
authors.initials: C
authors.lastname: Brossard
authors.affiliation: INRA, UR 1268 BIA (Biopolymers, Interactions, Assemblies), F-44316, rue de la Géraudière, 44316 Nantes, France.
authors.forename: S
authors.initials: S
authors.lastname: Denery-Papini
mesh_terms: D000485:Allergens / Q000737:chemistry / Q000276:immunology*; D000818:Animals; D017951:Antigen Presentation / Q000276:immunology; D001491:Basophils / Q000276:immunology; D002648:Child; D003296:Cooking; D021181:Egg Hypersensitivity / Q000276:immunology* / Q000517:prevention & control; D004529:Egg White / Q000009:adverse effects / Q000737:chemistry; D005260:Female; D006358:Hot Temperature; D006801:Humans; D007074:Immunoglobulin G / Q000097:blood; D051379:Mice; D010047:Ovalbumin / Q000737:chemistry / Q000276:immunology*; D018417:Th1 Cells / Q000276:immunology
chemical_list: D000485:Allergens; D007074:Immunoglobulin G; D010047:Ovalbumin
keywords: Aggregation; Basophil activation; Egg allergy; Food processing