The thermal aggregation of ovalbumin as large particles decreases its allergenicity for egg allergic patients and in a murine model.
Food Chem
; 203: 136-144, 2016 Jul 15.
Article
en En
| MEDLINE
| ID: mdl-26948598
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.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Alérgenos
/
Ovalbúmina
/
Culinaria
/
Hipersensibilidad al Huevo
/
Clara de Huevo
Límite:
Animals
/
Child
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Female
/
Humans
Idioma:
En
Revista:
Food Chem
Año:
2016
Tipo del documento:
Article
País de afiliación:
Francia