Nugraha Roni, Ruethers Thimo, Taki Aya C, Johnston Elecia B, Karnaneedi Shaymaviswanathan, Kamath Sandip D, Lopata Andreas L
Department of Aquatic Product Technology, Faculty of Fisheries and Marine Science, IPB University, Bogor 16680, Indonesia.
Molecular Allergy Research Laboratory, College of Public Health, Medical and Veterinary Sciences, James Cook University, Douglas 4811, Australia.
Foods. 2022 Jan 30;11(3):404. doi: 10.3390/foods11030404.
The Pacific oyster is a commercially important mollusc and, in contrast to most other shellfish species, frequently consumed without prior heat treatment. Oysters are rich in many nutrients but can also cause food allergy. Knowledge of their allergens and cross-reactivity remains very limited. These limitations make an optimal diagnosis of oyster allergy difficult, in particular to the Pacific oyster (), the most cultivated and consumed oyster species worldwide. This study aimed to characterise IgE sensitisation profiles of 21 oyster-sensitised patients to raw and heated Pacific oyster extract using immunoblotting and advanced mass spectrometry, and to assess the relevance of recombinant oyster allergen for improved diagnosis. Tropomyosin was identified as the major allergen recognised by IgE from 18 of 21 oyster-sensitised patients and has been registered with the WHO/IUIS as the first oyster allergen (Cra g 1). The IgE-binding capacity of oyster-sensitised patients' IgE to purified natural and recombinant tropomyosin from oyster, prawn, and dust mite was compared using enzyme-linked immunosorbent assay. The degree of IgE binding varied between patients, indicating partial cross-sensitisation and/or co-sensitisation. Amino acid sequence alignment of tropomyosin from these three species revealed five regions that contain predicted IgE-binding epitopes, which are most likely responsible for this cross-reactivity. This study fully biochemically characterises the first and major oyster allergen Cra g 1 and demonstrates that the corresponding recombinant tropomyosin should be implemented in improved component-resolved diagnostics and guide future immunotherapy.
太平洋牡蛎是一种具有重要商业价值的软体动物,与大多数其他贝类物种不同,它经常未经预先热处理就被食用。牡蛎富含多种营养成分,但也可能引发食物过敏。人们对其过敏原和交叉反应性的了解仍然非常有限。这些局限性使得对牡蛎过敏,尤其是对太平洋牡蛎(全球养殖和消费最多的牡蛎品种)进行最佳诊断变得困难。本研究旨在利用免疫印迹和先进的质谱技术,对21名对生的和加热后的太平洋牡蛎提取物过敏的患者的IgE致敏谱进行表征,并评估重组牡蛎过敏原在改进诊断方面的相关性。原肌球蛋白被确定为21名牡蛎致敏患者中18名患者的IgE所识别的主要过敏原,并已被世界卫生组织/国际免疫学会注册为第一种牡蛎过敏原(Cra g 1)。使用酶联免疫吸附测定法比较了牡蛎致敏患者的IgE对来自牡蛎、对虾和尘螨的纯化天然和重组原肌球蛋白的IgE结合能力。患者之间的IgE结合程度各不相同,表明存在部分交叉致敏和/或共同致敏。这三种物种的原肌球蛋白的氨基酸序列比对揭示了五个含有预测的IgE结合表位的区域,这些区域很可能是这种交叉反应性的原因。本研究对第一种也是主要的牡蛎过敏原Cra g 1进行了全面的生化表征,并表明相应的重组原肌球蛋白应应用于改进的组分解析诊断中,并指导未来的免疫治疗。