The thermal aggregation of ovalbumin as large particles decreases its allergenicity for egg allergic patients and in a murine model. (15th July 2016)

• Record Type: Journal Article
• Authors: Claude, M.; Lupi, R.; Bouchaud, G.; Bodinier, M.; Brossard, C.; Denery-Papini, S.
• Is Part Of: Food chemistry. Volume 203(2016)
• Page Start: 136
• Page End: 144
• Publication Date: 2016-07-15
• Subjects: A-OVA aggregated OVA -- EW egg whites -- IF mean intensity of fluorescence measured on coated OVA -- IF0 mean intensity of fluorescence measured without coated OVA -- LLS laser light scattering -- mMCP-1 mouse mast cell protease-1 -- N-OVA native OVA -- OVA ovalbumin -- OVM ovomucoid -- RBL Rat basophil leukemia; Aggregation -- Basophil activation -- Egg allergy -- Food processing; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2016.02.054
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: The allergenicity of native and large aggregates of ovalbumin was investigated. Heat aggregation enhanced IgG production and induced a pro Th1-profile. Large aggregates displayed lower Ig-binding in man or mouse. Large aggregates had reduced basophil activation capacities in man or mouse. 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.