Motoyama K, Ishizaki S, Nagashima Y, Shiomi K
Department of Food Science and Technology, Tokyo University of Marine Science and Technology, Konan-4, Minato-ku, Tokyo 108-8477, Japan.
Food Chem Toxicol. 2006 Dec;44(12):1997-2002. doi: 10.1016/j.fct.2006.06.018. Epub 2006 Jul 10.
Heated extracts prepared from the mantle muscles (for decapods) or leg muscles (for octapods) of nine species of cephalopods were shown to be all reactive with serum IgE in crustacean-allergic patients. No marked difference in the reactivity with IgE was recognized among the cephalopods, suggesting that they are almost equally allergenic. Immunoblotting and inhibition immunoblotting data revealed that the major allergen is tropomyosin in common with the nine species of cephalopods and that the cephalopod tropomyosins are cross-reactive with one another and also with crustacean tropomyosins. Molecular cloning experiments first elucidated the primary structures of tropomyosins from five species of cephalopods. The cephalopod tropomyosins show high sequence identity (more than 92% identity) with one another, being the molecular basis for their cross-reactivity. Although the sequence identity between cephalopod and crustacean topomyosins is only about 63-64%, some of the IgE-binding epitopes proposed for brown shrimp Penaeus aztecus tropomyosin (Pen a 1) are well conserved in the cephalopod tropomyosins, supporting the cross-reactivity between cephalopod and crustacean tropomyosins.
研究表明,从9种头足类动物的外套膜肌肉(十足目)或腿部肌肉(八足目)制备的热提取物,对甲壳类过敏患者的血清IgE均有反应。在所研究的头足类动物中,未发现与IgE反应性有明显差异,这表明它们的致敏性几乎相同。免疫印迹和抑制免疫印迹数据显示,主要过敏原是原肌球蛋白,9种头足类动物都有这种情况,而且头足类原肌球蛋白之间以及与甲壳类原肌球蛋白之间存在交叉反应。分子克隆实验首次阐明了5种头足类动物原肌球蛋白的一级结构。头足类原肌球蛋白之间显示出高度的序列同一性(同一性超过92%),这是它们交叉反应的分子基础。虽然头足类和甲壳类原肌球蛋白之间的序列同一性仅约为63%-64%,但一些针对褐虾(Penaeus aztecus)原肌球蛋白(Pen a 1)提出的IgE结合表位在头足类原肌球蛋白中得到了很好的保留,这支持了头足类和甲壳类原肌球蛋白之间的交叉反应。