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Removal and Replacement of Endogenous Ligands from Lipid-Bound Proteins and Allergens
Published on: February 24, 2021
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Bos d 13, A Novel Heat-Stable Beef Allergen.
Patricia Román-Carrasco1, Christoph Klug1,2, Wolfgang Hemmer3
1Biotechnology Section, FH Campus Wien, Campus Vienna Biocenter, University of Applied Sciences, Vienna, 1100, Austria.
Molecular Nutrition & Food Research
|May 13, 2023
Summary
Myosin light chains (MYLs) are identified as novel allergens in cooked beef, causing IgE-mediated allergic reactions. These heat-stable proteins, MYL1 and MYL3, show potential for intestinal sensitization.
Area of Science:
- Food allergy research
- Immunology
- Proteomics
Background:
- Red meat consumption is widespread, but specific allergens beyond serum albumin and alpha-Gal remain largely unidentified.
- IgE-mediated allergic reactions to red meat are a growing concern.
Purpose of the Study:
- To identify novel allergens in beef responsible for IgE-mediated allergic reactions.
- To characterize the properties and potential sensitizing capacity of identified allergens.
Main Methods:
- IgE-immunoblotting of beef extracts from individuals sensitized to beef.
- Peptide mass fingerprinting to identify IgE-reactive proteins.
- Recombinant protein production and characterization (ELISA, circular dichroism, in vitro digestion).
- Assessment of intestinal epithelial cell permeability.
Main Results:
- Two IgE-reactive proteins, myosin light chain 1 (MYL1) and myosin light chain 3 (MYL3), were identified in cooked beef.
- Recombinant MYL1 and MYL3 (rMYL1, rMYL3) demonstrated IgE reactivity and significant thermal stability.
- rMYL1 exhibited higher stability during in vitro digestion and was capable of crossing intestinal epithelial cells without compromising tight junctions.
Conclusions:
- Myosin light chains (MYLs) are identified as novel, heat-stable allergens in bovine meat.
- MYL1 and MYL3 are significant contributors to red meat allergy.
- MYL1 possesses characteristics suggesting a potential role in meat allergy sensitization.
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