TY - JOUR
T1 - Bos d 13, A Novel Heat-Stable Beef Allergen
AU - Román-Carrasco, Patricia
AU - Klug, Christoph
AU - Hemmer, Wolfgang
AU - Focke-Tejkl, Margarete
AU - Raith, Marianne
AU - Grosinger, Isabella
AU - Stoll, Peter
AU - Quirce, Santiago
AU - Sanchez-Jareño, Marta
AU - Martínez-Blanco, Mónica
AU - Molina, Elena
AU - Somoza, Veronika
AU - Lieder, Barbara
AU - Marin, Zana
AU - Nöbauer, Katharina
AU - Hummel, Karin
AU - Razzazi-Fazeli, Ebrahim
AU - Swoboda, Ines
N1 - Accession Number: WOS:001017627700001
PubMed ID: 37173826
PY - 2023/8
Y1 - 2023/8
N2 - Scope: Red 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 results: IgE 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. Conclusion: MYLs are identified as novel heat-stable bovine meat allergens.
AB - Scope: Red 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 results: IgE 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. Conclusion: MYLs are identified as novel heat-stable bovine meat allergens.
KW - allergens
KW - heat stability
KW - meat allergy
KW - myosin light chain
KW - recombinant allergens
KW - red meat
KW - stability to digestion
UR - http://www.scopus.com/inward/record.url?scp=85163633496&partnerID=8YFLogxK
U2 - 10.1002/mnfr.202200601
DO - 10.1002/mnfr.202200601
M3 - Article
AN - SCOPUS:85163633496
SN - 1613-4125
VL - 67
JO - Molecular Nutrition and Food Research
JF - Molecular Nutrition and Food Research
IS - 16
M1 - 2200601
ER -