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Bos d 13, a novel heat-stable beef allergen.

SCOPE: Red meat is a staple food of Western diets, but it can also induce IgE-mediated allergic reactions. Yet, apart from the heat-labile protein serum albumin and the carbohydrate α-Gal, the molecules involved in allergic reactions to red meat remain unknown.

METHODS AND RESULTS: IgE reactivity profiles of beef-sensitized individuals were analyzed by IgE-immunoblotting with protein extracts from raw and cooked beef. IgE-reactive proteins were identified by peptide mass fingerprinting. Bovine myosin light chains (MYLs) were produced recombinantly. IgE reactivity of the recombinant allergens was analyzed by ELISA and the molecules' fold evaluated by circular dichroism analysis. The stability of the proteins to gastrointestinal digestion was investigated in vitro. The transport of recombinant myosin light chain 1 (rMYL1) through the intestinal epithelium was evaluated by exposing a monolayer of Caco-2 cells to rMYL1. Two IgE-reactive proteins were identified as myosin light chain 1 (MYL1) and myosin light chain 3 (MYL3) in the cooked-beef extract and were designated Bos d 13 isoallergens. rMYL1 and rMYL3 represent folded, IgE reactive proteins and they both display remarkable thermal stability. rMYL1 showed higher resistance to gastrointestinal digestion than rMYL3 and was able to cross a monolayer of intestinal cells without disturbing the integrity of the tight junctions, suggesting the sensitizing capacity of MYL1.

CONCLUSION: MYLs were identified as novel heat-stable bovine meat allergens. This article is protected by copyright. All rights reserved.

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