High-resolution mass spectrometry unveils the molecular changes of ovalbumin induced by heating and their influence on IgE binding capacity.
Food Chem
; 395: 133624, 2022 Nov 30.
Article
en En
| MEDLINE
| ID: mdl-35820272
ABSTRACT
Ovalbumin (OVA) is a food allergen whose allergenicity is modulated by heating. We aimed to establish a molecular connection between heat-induced structural 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.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Inmunoglobulina E
/
Hipersensibilidad a los Alimentos
Límite:
Humans
Idioma:
En
Revista:
Food Chem
Año:
2022
Tipo del documento:
Article
País de afiliación:
Francia