High-resolution mass spectrometry unveils the molecular changes of ovalbumin induced by heating and their influence on IgE binding capacity - INRAE - Institut national de recherche pour l’agriculture, l’alimentation et l’environnement Accéder directement au contenu
Article Dans Une Revue Food Chemistry Année : 2022

High-resolution mass spectrometry unveils the molecular changes of ovalbumin induced by heating and their influence on IgE binding capacity

Résumé

Ovalbumin (OVA) is a food allergen whose allergenicity is modulated by heating. We aimed to establish a molecular connection between heat-induced modifications and the modulation of the IgE binding capacity of OVA. For this, we used model samples of heat-modified OVA with increasing complexity; glycated, aggregated or glycated and aggregated. Using sera from egg-allergic individuals, we show that both aggregation and glycation strongly impacted IgE binding capacity, despite limited structural changes for glycated OVA. A molecular exploration at the amino acid level using high-resolution mass spectrometry = revealed extensive cross-linking, mostly through disulfide and dehydroprotein bridges, and moderate but significant glycation. Structural modifications affected residues located within or at a few amino acids distance of known human linear IgE epitopes, such as C121, K123, S169, K190, K207, H332 and C368. We thus unveil key amino residues implicated in the changes in IgE binding of OVA induced by heating
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hal-03717804 , version 1 (08-07-2022)

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Paternité - Pas d'utilisation commerciale - Pas de modification

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Mehdi Cherkaoui, Dominique Tessier, Virginie Lollier, Colette Larré, Chantal Brossard, et al.. High-resolution mass spectrometry unveils the molecular changes of ovalbumin induced by heating and their influence on IgE binding capacity. Food Chemistry, 2022, 395, pp.133624. ⟨10.1016/j.foodchem.2022.133624⟩. ⟨hal-03717804⟩

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