How Proteins Aggregate Can Reduce Allergenicity: Comparison of Ovalbumins Heated under Opposite Electrostatic Conditions

• Published in: Journal of agricultural and food chemistry 2017-05, Vol.65 (18), p.3693-3701
• Main Authors: Claude, Mathilde, Bouchaud, Grégory, Lupi, Roberta, Castan, Laure, Tranquet, Olivier, Denery-Papini, Sandra, Bodinier, Marie, Brossard, Chantal
• Format: Article
• Language: English
• Subjects: Allergens - chemistry; Allergens - immunology; Animals; Basophils - immunology; Egg Hypersensitivity - immunology; Female; Hot Temperature; Humans; Immunoglobulin G - immunology; Life Sciences; Mice; Mice, Inbred BALB C; Ovalbumin - chemistry; Ovalbumin - immunology; Protein Aggregates; Rats; Static Electricity
• ISSN: 0021-8561; 1520-5118
• DOI: 10.1021/acs.jafc.7b00676

Heated foods are recommended for avoiding sensitization to food proteins, but depending on the physicochemical conditions during heating, more or less unfolded proteins aggregate differently. Whether the aggregation process could modulate allergenicity was investigated. Heating ovalbumin in opposite electrostatic conditions led to small (A-s, about 50 nm) and large (A-L, about 65 μm) aggregates that were used to sensitize mice. The symptoms upon oral challenge and rat basophil leukemia degranulation with native ovalbumin differed on the basis of which aggregates were used during the sensitization. Immunoglobulin-E (IgE) production was significantly lower with A-s than with A-L. Although two common linear IgE-epitopes were found, the aggregates bound and cross-linked IgE similarly or differently, depending on the sensitizing aggregate. The ovalbumin aggregates thus displayed a lower allergenic potential when formed under repulsive rather than nonrepulsive electrostatic conditions. This further demonstrates that food structure modulates the immune response during the sensitization phase with some effects on the elicitation phase of an allergic reaction and argues for the need to characterize the aggregation state of allergens.