Xiao Yucheng, Tang Jianzhou, Hu Weijun, Xie Jinyun, Maertens Chantal, Tytgat Jan, Liang Songping
College of Life Sciences, Hunan Normal University, Changsha 410081, China.
J Biol Chem. 2005 Apr 1;280(13):12069-76. doi: 10.1074/jbc.M411651200. Epub 2004 Nov 17.
Jingzhaotoxin-I (JZTX-I), a 33-residue polypeptide, is derived from the Chinese tarantula Chilobrachys jing-zhao venom based on its ability to evidently increase the strength and the rate of vertebrate heartbeats. The toxin has three disulfide bonds with the linkage of I-IV, II-V, and III-VI that is a typical pattern found in inhibitor cystine knot molecules. Its cDNA determined by rapid amplification of 3'- and 5'-cDNA ends encoded a 62-residue precursor with a small proregion of eight residues. Whole-cell configuration indicated that JZTX-I was a novel neurotoxin preferentially inhibiting cardiac sodium channel inactivation by binding to receptor site 3. Although JZTX-I also exhibits the interaction with channel isoforms expressing in mammalian and insect sensory neurons, its affinity for tetrodotoxin-resistant subtype in mammalian cardiac myocytes (IC50 = 31.6 nm) is approximately 30-fold higher than that for tetrodotoxin-sensitive subtypes in latter tissues. Not affecting outward delay-rectified potassium channels expressed in Xenopus laevis oocytes and tetrodotoxin-resistant sodium channels in mammal sensory neurons, JZTX-I hopefully represents a potent ligand to discriminate cardiac sodium channels from neuronal tetrodotoxin-resistant isoforms. Furthermore, different from any reported spider toxins, the toxin neither modifies the current-voltage relationships nor shifts the steady-state inactivation of sodium channels. Therefore, JZTX-I defines a new subclass of spider sodium channel toxins. JZTX-I is an alpha-like toxin first reported from spider venoms. The result provides an important witness for a convergent functional evolution between spider and other animal venoms.
敬钊毒素-I(JZTX-I)是一种由33个氨基酸残基组成的多肽,它源自中国捕鸟蛛敬钊缨毛蛛的毒液,因为它能够显著增强脊椎动物心跳的强度和速率。该毒素具有三条二硫键,连接方式为I-IV、II-V和III-VI,这是在抑制性胱氨酸结分子中发现的典型模式。通过3'-和5'-cDNA末端的快速扩增确定的其cDNA编码一个62个氨基酸残基的前体,带有一个由八个氨基酸残基组成的小前导区。全细胞模式表明JZTX-I是一种新型神经毒素,它通过与受体位点3结合优先抑制心脏钠通道失活。尽管JZTX-I也表现出与在哺乳动物和昆虫感觉神经元中表达的通道亚型的相互作用,但其对哺乳动物心肌细胞中耐河豚毒素亚型的亲和力(IC50 = 31.6 nM)比对后一种组织中对河豚毒素敏感亚型的亲和力高约30倍。JZTX-I不影响非洲爪蟾卵母细胞中表达的外向延迟整流钾通道和哺乳动物感觉神经元中的耐河豚毒素钠通道,有望成为一种有效的配体,用于区分心脏钠通道和神经元耐河豚毒素亚型。此外,与任何已报道的蜘蛛毒素不同,该毒素既不改变电流-电压关系,也不改变钠通道的稳态失活。因此,JZTX-I定义了蜘蛛钠通道毒素的一个新亚类。JZTX-I是首次从蜘蛛毒液中报道的一种α-样毒素。该结果为蜘蛛毒液与其他动物毒液之间的趋同功能进化提供了重要证据。