嗜碱性粒细胞活化
粉虱
食物过敏
原肌球蛋白
过敏原
屋尘螨
过敏
交叉反应性
免疫球蛋白E
生物
食品科学
嗜碱性粒细胞
免疫学
生物化学
生态学
抗体
交叉反应
幼虫
肌球蛋白
作者
K.C.M. Verhoeckx,Sarah van Broekhoven,Marco Gaspari,SC de Hartog-Jager,Govardus de Jong,Harry J. Wichers,Els van Hoffen,Geert F. Houben,André C. Knulst
标识
DOI:10.1186/2045-7022-3-s3-p48
摘要
Background Due to the imminent growth of the world population, shortage of protein sources for human consumption will arise in the near future. Alternative and sustainable protein sources (e.g. insects and algae) are now being explored for the production of food and feed. In this project the safety of mealworm (Tenebrio molitor L.) proteins for human consumption was tested according to the European Food Safety Authority (EFSA) [1] guidelines for allergenicity risk assessment of genetically modified organisms (GMO). Methods Different mealworm protein fractions (soluble and insoluble) were prepared, characterized, and tested for cross-reactivity using IgE from patients with an inhalation or food allergy to closely related species (house dust mite and crustacean) according to the phylogenetic tree, using immunoblotting and indirect basophil activation. Furthermore, the stability was investigated using an in vitro pepsin digestion test. Results IgE from both house dust mite and crustacean allergic patients cross-reacted with proteins in mealworm. This cross-reactivity was functional, as shown by the induction of basophil activation. The cross-reactive proteins were identified as tropomyosin and arginine kinase, which are well known allergens in lobster, shrimp and house dust mite. These proteins were mildly stable in the pepsin stability test. Conclusion
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