Biotechnology Section, FH Campus Wien, Campus Vienna Biocenter, University of Applied Sciences, Vienna, 1100, Austria.
Present address: MacroArray Diagnostics GmbH, Vienna, 1230, Austria.
Mol Nutr Food Res. 2023 Aug;67(16):e2200601. doi: 10.1002/mnfr.202200601. Epub 2023 Jun 30.
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.
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.
MYLs are identified as novel heat-stable bovine meat allergens.
红肉是西方饮食中的主食，也可能引起 IgE 介导的过敏反应。然而，除了热不稳定的血清白蛋白和碳水化合物 α-Gal 之外，引起红肉过敏的分子仍然未知。
通过用生肉和熟肉的蛋白质提取物进行 IgE-免疫印迹分析，分析牛肉过敏个体的 IgE 反应谱。通过肽质量指纹图谱将两种 IgE 反应蛋白鉴定为烹饪牛肉提取物中的肌球蛋白轻链 1（MYL1）和肌球蛋白轻链 3（MYL3），并指定为 Bos d 13 同种异体过敏原。MYL1 和 MYL3 在大肠杆菌中重组产生。ELISA 证明了它们的 IgE 反应性，圆二色性分析表明它们代表具有显著热稳定性的折叠分子。与 rMYL3 相比，体外胃肠道消化实验表明 rMYL1 具有更高的稳定性。rMYL1 暴露于单层 Caco-2 细胞表明该分子能够穿过肠上皮细胞而不破坏紧密连接的完整性，这表明 MYL1 具有致敏能力。
肌球蛋白被鉴定为新型耐热牛肉过敏原。
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