Molecular cloning of serine proteases from elapid snake venoms
Molecular cloning of serine proteases from elapid snake venoms
复制标题
蛇毒丝氨酸蛋白酶的分子克隆。
DOI：
10.1016/j.toxicon.2007.02.013
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发表时间：
2007-06-15
期刊：
影响因子：
2.8
通讯作者：
Zhang, Yun
中科院分区：
文献类型：
--
作者：
Jin, Yang;Lee, Wen-Hui;Zhang, Yun
丝氨酸蛋白酶在蝰蛇毒液中广泛分布，但在眼镜蛇毒液中罕见。此前，我们从眼镜王蛇（Ophiophagus hannah）的毒液中鉴定出一种名为OhS1的纤维蛋白原溶解酶。结果表明OhS1可能是一种丝氨酸蛋白酶，但之前没有结构方面的证据。在本研究中，通过蛋白质测序，并结合逆转录聚合酶链反应（RT - PCR）和5' - 快速扩增cDNA末端（5' - RACE）方法确定了OhS1的一级结构。OhS1前体由一个18个氨基酸的信号肽、一个6个氨基酸的假定激活肽和236个氨基酸的成熟蛋白组成。来自舟山眼镜蛇（Naja atra）和银环蛇（Bungarus multicinctus）的OhS1同源物也被克隆并报道。这些眼镜蛇毒液丝氨酸蛋白酶与蝰科和游蛇科蛇毒中的丝氨酸蛋白酶呈现出约60%的序列同一性。系统发育分析表明蛇毒丝氨酸蛋白酶可能有一个共同的祖先。（c）2007爱思唯尔有限公司。保留所有权利。
Serine proteases are widely distributed in viperid snake venoms, but rare in elapid snake venoms. Previously, we have identified a fibrinogenolytic enzyme termed OhS1 from the venom of Ophiophagus hannah. The results indicated that OhS1 might be a serine protease, but there was no structural evidence previously. In the present study, the primary structure of OhS1 was determined by protein sequencing, in combination with RT-PCR and 5'-RACE methods. OhS1 precursor is composed of an 18-amino acid signal peptide, a 6-amino acid putative activation peptide and 236-amino acid mature protein. OhSI homologues from Naja atra and Bungarus multicinctus were also cloned and reported. These elapid venom serine proteases exhibited similar to 60% sequence identity with serine proteases from the snake venoms of the Viperidae and Colubridae family. Phylogenetic analysis indicated that snake venom serine protease might have a common ancestor. (c) 2007 Elsevier Ltd. All rights reserved.