Chemical and biochemical study on venomous jellyfish proteinaceous toxins

刺胞动物门的成员（珊瑚，海葵，刺鱼）装备有线虫囊（刺细胞），它们用于捕获猎物和防御。许多刺胞动物被认为是危险的海洋生物，因为它们的毒刺造成的毒性。有报道称，一些刺尾鱼，如Chironex fleckeri、四条鳍叉尾鱼和酸浆属酸浆的螫刺对人类是致命的。刺胞动物毒素已被广泛研究，其化学特征主要是蛋白质。由于其不稳定的性质，刺胞动物毒素的确切化学性质尚未阐明，除了一些来自海葵的适度稳定的神经毒性多肽。最近，我们已经开发了一种新的纯化方法，从水母中分离不稳定的蛋白质类毒素。这种纯化方法已导致从三种箱鲀（海黄蜂），Carybdea rastoni，Carybdea alota和Chropslmus quadrigatus中分离出活性蛋白毒素。C.拉斯托尼是日本最讨厌的海洋生物之一，游泳和洗澡。C.阿拉塔是一种常见的刺在夏威夷。这三个物种的刺痛已被记录为引起人类皮肤疼痛和炎症。据报道，C。冲绳的quadrigatus导致三人死亡。采用RT-PCR和5 '-/3'-RACE方法对分离的C. rastoni、阿拉塔C.三种鱼类的蛋白质类毒素（43-45 kDa）之间的比较显示出22-44%的同源性。由于这些毒素没有显示出与任何其他已知蛋白质的任何同源性，这表明这些毒素代表了一类新的生物活性蛋白。

Members of the phylum Cnidaria (corals, sea anemones, jellyfishes) are equipped with nemaotocysts (stinging cells) which they use in capturing prey and for defense. Many cnidarians are considered hazardous sea-creatures due to the toxicity inflicted by their sting. The sting of some jellyfishes, such as Chironex fleckeri, Chropsalmus quadrigatus and Physalia Physalis have been reported to be lethal to humans. Cnidarian toxins have been extensively studied and chemically characterized as mostly proteinaceous. The exact chemical properties of cnidarian toxins have not been elucidated due to their labile nature, except for some moderately stable neurotoxic polypeptides from sea anemones. Recently, we have developed a novel purification method for isolating unstable proteinaceous toxins from jellyfish. This purification method has resulted in the isolation of active protein toxins from three species of box jellyfishes (sea wasps), Carybdea rastoni, Carybdea alota and Chropslmus quadrigatus. C. rastoni is one of the most annoying sea-creatures for swimmers and bathers in Japan. C. alata is a common stinger in Hawaii. The sting of these three Species has been documented to induce cutaneous pain and inflammation in humans. Lt has been reported that the sting of C. quadrigatus from Okinawan resulted in three fatalities. RT-PCR and 5'-/3'-RACE methods were used to elucidate the full-length nucleotide and amino acid sequences of the isolated proteinaceous toxins from C. rastoni, C alata and C. quadrigatus Comparison between the proteinaceous toxins (43-45 kDa) from the three jellyfishes demonstrated 22-44% homology. Since these toxins did not show any homology with any other known protein, it is suggested that these toxins represent a novel class of bioastie proteins.