ArticleMolecular nutrition & food research2023
Bos d 13, A Novel Heat-Stable Beef Allergen.
Article in Molecular nutrition & food research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Meat allergy: Specific reactions to chicken, beef, pork, and alternative protein sources.Asia Pacific allergy · 2026Review
- Increased risk of IgE-mediated allergies in patients with celiac disease: a case-control study.Frontiers in nutrition · 2025Article
- Treatment of Allergies to Fur Animals.International journal of molecular sciences · 2024Review
- Genomics of Shrimp Allergens and Beyond.Genes · 2023Review
- Bos d 13, A Novel Heat-Stable Beef Allergen.Molecular nutrition & food research · 2023Article
Corrections and comments
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Authors and funding
18 authors at 7 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.