Bos d 13, A Novel Heat‐Stable Beef Allergen

Author:

Román‐Carrasco Patricia1,Klug Christoph12,Hemmer Wolfgang3,Focke‐Tejkl Margarete4ORCID,Raith Marianne1,Grosinger Isabella1,Stoll Peter1,Quirce Santiago5,Sanchez‐Jareño Marta5,Martínez‐Blanco Mónica6,Molina Elena6,Somoza Veronika78ORCID,Lieder Barbara7ORCID,Marin Zana1,Nöbauer Katharina9,Hummel Karin9,Razzazi‐Fazeli Ebrahim9,Swoboda Ines14ORCID

Affiliation:

1. Biotechnology Section FH Campus Wien Campus Vienna Biocenter University of Applied Sciences Vienna 1100 Austria

2. Present address: MacroArray Diagnostics GmbH Vienna 1230 Austria

3. FAZ‐Floridsdorf Allergy Center Vienna 1210 Austria

4. Division of Immunopathology Department of Pathophysiology and Allergy Research Center for Pathophysiology Infectiology and Immunology Medical University of Vienna Vienna 1090 Austria

5. Department of Allergy La Paz University Hospital, IdiPAZ Madrid 28046 Spain

6. Instituto de Investigación en Ciencias de la Alimentación (CIAL, CSIC‐UAM) Madrid 28049 Spain

7. Department of Physiological Chemistry Faculty of Chemistry University of Vienna Vienna 1090 Austria

8. Leibniz Institute for Food Systems Biology Technical University Munich 85354 Munich Germany

9. VetCore Facility for Research University of Veterinary Medicine Vienna 1210 Austria

Abstract

ScopeRed meat, a staple food of Western diets, can also induce IgE‐mediated allergic reactions. Yet, apart from the heat‐labile protein serum albumin and the carbohydrate α‐Gal, the molecules causing allergic reactions to red meat remain unknown.Methods and resultsIgE reactivity profiles of beef‐sensitized individuals are analyzed by IgE‐immunoblotting with protein extracts from raw and cooked beef. Two IgE‐reactive proteins are identified by peptide mass fingerprinting as myosinlight chain 1 (MYL1) and myosin light chain 3 (MYL3) in cooked beef extract and are designated Bos d 13 isoallergens. MYL1 and MYL3 are produced recombinantly in Escherichia coli. ELISAs proved their IgE reactivity and circular dichroism analysis showed that they represent folded molecules with remarkable thermal stability. In vitro gastrointestinal digestion experiments showed the higher stability of rMYL1 as compared to rMYL3. Exposure of a monolayer of Caco–2 cells to rMYL1 indicated that the molecule is able to cross intestinal epithelial cells without disturbing the integrity of the tight junctions, suggesting the sensitizing capacity of MYL1.ConclusionMYLs are identified as novel heat‐stable bovine meat allergens.

Funder

Austrian Science Fund

Publisher

Wiley

Subject

Food Science,Biotechnology

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