Jiang Hui, Wang Cheng-Zhong, Xu Chen-Qi, Fan Chong-Xu, Dai Xian-Dong, Chen Ji-Sheng, Chi Cheng-Wu
Shanghai Institute of Biochemistry and Cell Biology, Shanghai Institute of Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.
Peptides. 2006 Apr;27(4):682-9. doi: 10.1016/j.peptides.2005.08.004. Epub 2005 Sep 21.
Cone snails are tropical marine mollusks that envenomate prey with a complex mixture of neuropharmacologically active compounds for the purpose of feeding and defence, each evolved to act in a highly specific manner on different parts of the nervous system. Here, we report the peptide purification, molecular cloning, chemical synthesis, and functional characterization of a structurally unique toxin isolated from the venom of Conus vexillum. The novel peptide, designated Vx2, was composed of 21 amino acid residues cross-linked by 3 disulfide bonds (WIDPSHYCCCGGGCTDDCVNC). Intriguingly, its mature peptide sequence shows low level of similarity with other identified conotoxins, and its unique motif (-CCCGGGC-) was not reported in other Conus peptides. However, its signal peptide sequence shares high similarity with those of the M-superfamily conotoxins. Hence, Vx2 could be classified into a new family of the M-superfamily.
芋螺是热带海洋软体动物，它们会用一系列复杂的具有神经药理活性的化合物来麻痹猎物，以达到捕食和防御的目的，每一种化合物都进化为以高度特异性的方式作用于神经系统的不同部位。在此，我们报告了从织锦芋螺毒液中分离出的一种结构独特的毒素的肽纯化、分子克隆、化学合成及功能表征。这种新型肽被命名为Vx2，由21个氨基酸残基组成，通过3个二硫键交联（WIDPSHYCCCGGGCTDDCVNC）。有趣的是，其成熟肽序列与其他已鉴定的芋螺毒素相似度较低，且其独特基序（-CCCGGGC-）在其他芋螺肽中未被报道。然而，其信号肽序列与M超家族芋螺毒素的信号肽序列高度相似。因此，Vx2可被归类为M超家族的一个新家族。
