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Digested Ara h 1 has sensitizing capacity in Brown Norway rats

Summary Background Food allergies are a public health issue of growing concern, with peanuts in particular being associated with severe reactions. The peanut allergen, Ara h 1, belongs to the cupin plant food allergen family, which, unlike other structural families, appears to be broken down rapidly...

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Bibliographic Details
Published in:Clinical and experimental allergy 2009-10, Vol.39 (10), p.1611-1621
Main Authors: Bøgh, K. L., Kroghsbo, S., Dahl, L., Rigby, N. M., Barkholt, V., Mills, E. N. C., Madsen, C. B.
Format: Article
Language:English
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Summary:Summary Background Food allergies are a public health issue of growing concern, with peanuts in particular being associated with severe reactions. The peanut allergen, Ara h 1, belongs to the cupin plant food allergen family, which, unlike other structural families, appears to be broken down rapidly following gastrointestinal digestion. Objective Using Ara h 1 as a model allergen, the ability of digested protein to sensitize has been investigated. Methods Ara h 1 was purified from whole roasted peanuts. Intact Ara h 1 was digested in an in vitro model, simulating the human gastrointestinal digestion process. Digestion products were analysed for peptide sizes and their ability to aggregate. Brown Norway (BN) rats, used as an animal model, were immunized with purified intact Ara h 1 or the gastrointestinal digestion products thereof. The sensitizing capacity was evaluated by analyses of specific antibody (IgG1, IgG2a and IgE) responses and ability to trigger mediator release of rat basophilic leukaemia (RBL)‐2H3 cells. Results The present study showed that Ara h 1 was broken down, resulting in peptide fragments of sizes
ISSN:0954-7894
1365-2222
DOI:10.1111/j.1365-2222.2009.03333.x