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Identification of tropomyosins as major allergens in antarctic krill and mantis shrimp and their amino Acid sequence characteristics

机译:原养肌原蛋白作为南极磷虾和螳螂虾主要过敏原的鉴定及其氨基酸序列特征

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Tropomyosin represents a major allergen of decapod crustaceans such as shrimps and crabs, and its highly conserved amino acid sequence (>90% identity) is a molecular basis of the immunoglobulin E (IgE) cross-reactivity among decapods. At present, however, little information is available about allergens in edible crustaceans other than decapods. In this study, the major allergen in two species of edible crustaceans, Antarctic krill Euphausia superba and mantis shrimp Oratosquilla oratoria that are taxonomically distinct from decapods, was demonstrated to be tropomyosin by IgE-immunoblotting using patient sera. The cross-reactivity of the tropomyosins from both species with decapod tropomyosins was also confirmed by inhibition IgE immunoblotting. Sequences of the tropomyosins from both species were determined by complementary deoxyribonucleic acid cloning. The mantis shrimp tropomyosin has high sequence identity (>90% identity) with decapod tropomyosins, especially with fast-type tropomyosins. On the other hand, the Antarctic krill tropomyosin is characterized by diverse alterations in region 13-42, the amino acid sequence of which is highly conserved for decapod tropomyosins, and hence, it shares somewhat lower sequence identity (82.4-89.8% identity) with decapod tropomyosins than the mantis shrimp tropomyosin. Quantification by enzyme-linked immunosorbent assay revealed that Antarctic krill contains tropomyosin at almost the same level as decapods, suggesting that its allergenicity is equivalent to decapods. However, mantis shrimp was assumed to be substantially not allergenic because of the extremely low content of tropomyosin.
机译:Tropomyosin代表十足类甲壳动物(如虾和蟹)的主要变应原,其高度保守的氨基酸序列(> 90%相同)是十足类动物之间免疫球蛋白E(IgE)交叉反应的分子基础。但是,目前,除了十足动物以外,鲜有关于可食用甲壳类中过敏原的信息。在这项研究中,使用患者血清通过IgE免疫印迹法在分类学上与两种动物的甲壳类动物(南极磷虾Euphausia superba和螳螂虾Oratosquilla Oratoria)的主要过敏原是原肌球蛋白。通过抑制IgE免疫印迹也证实了两种物种的原肌球蛋白与十足原肌球蛋白的交叉反应性。通过互补的脱氧核糖核酸克隆确定来自两种物种的原肌球蛋白的序列。螳螂虾原肌球蛋白与十足原肌球蛋白具有高度序列同一性(> 90%相同性),特别是与快型原肌球蛋白具有高度的序列同一性。另一方面,南极磷虾原肌球蛋白的特征是在13-42区有多种变化,其氨基酸序列对于十足原肌球蛋白高度保守,因此,其与南极磷虾原肌球蛋白的序列同一性较低(82.4-89.8%相同)。十足原肌球蛋白比螳螂虾原肌球蛋白高。通过酶联免疫吸附测定的定量显示,南极磷虾所含的原肌球蛋白水平几乎与十足动物相同,表明其致敏性与十足动物相同。但是,由于原肌球蛋白含量极低,因此认为螳螂虾基本上没有致敏性。

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