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首页> 外文期刊>Biochemistry >Characterization of a novel peptide toxin from acanthoscurria paulensis spider venom: A distinct cysteine assignment to the HWTX-II family
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Characterization of a novel peptide toxin from acanthoscurria paulensis spider venom: A distinct cysteine assignment to the HWTX-II family

机译：刺五加蜘蛛毒的新型肽毒素的表征：HWTX-II家族的一个独特的半胱氨酸分配

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摘要

Spider venom toxins have raised interest in prospecting new drugs and pesticides. Nevertheless, few studies are conducted with tarantula toxins, especially with species found in Brazil. This study aims to characterize chemically and biologically the first toxin isolated from Acanthoscurria paulensis venom. Ap1a consists of 48 amino acid residues and has a molecular mass of 5457.79 Da. The cloned gene encodes a putative sequence of 23 amino acid residues for the signal peptide and 27 for the pro-peptide. The sequence of the mature peptide is 60-84% identical with those of toxins of the HWTX-II family. Different from the structural pattern proposed for these toxins, the disulfide pairing of Ap1a is of the ICK type motif, which is also shared by the U1-TRTX-Bs1a toxin. Ap1a induced a dose-dependent and reversible paralytic effect in Spodoptera frugiperda caterpillars, with an ED_(50) of 13.0 ± 4.2 μg/g 8 h after injections. In the Drosophila melanogaster Giant Fiber circuit, Ap1a (1.14-22.82 μg/g) reduces both the amplitude and frequency of responses from GF-TTM and GF-DLM pathways, suggesting an action at the neuromuscular junction, which is mediated by glutamatergic receptors. It is also lethal to mice (1.67 μg/g, intracranial route), inducing effects similar to those reported with intracerebroventricular administration of NMDA. Ap1a (1 μM) does not alter the response induced by acetylcholine on the rhabdomyosarcoma cell preparation and shows no significant effects on hNa _v1.2, hNa_v1.4, hNa_v1.5, and hNa_v1.6 channels. Because of its unique sequence and cysteine assignment to the HWTX-II family, Ap1a is a significant contribution to the structure-function study of this family of toxins.
机译：蜘蛛毒毒素引起了人们对寻找新药和杀虫剂的兴趣。但是，很少有关于狼蛛毒素的研究，尤其是在巴西发现的物种。这项研究的目的是化学和生物学上表征从泡桐棘毒中分离出的第一毒素。 Ap1a由48个氨基酸残基组成，分子量为5457.79 Da。克隆的基因编码信号肽的23个氨基酸残基和前肽的27个氨基酸残基的假定序列。成熟肽的序列与HWTX-II家族的毒素的序列具有60-84％相同。与针对这些毒素提出的结构模式不同，Ap1a的二硫键配对具有ICK类型的基序，U1-TRTX-Bs1a毒素也具有这种模式。 Ap1a诱导草地贪夜蛾的剂量依赖性和可逆性麻痹作用，注射后8 h的ED_（50）为13.0±4.2μg/ g。在果蝇黑巨人纤维回路中，Ap1a（1.14-22.82μg/ g）降低了GF-TTM和GF-DLM途径的响应幅度和频率，表明对神经肌肉接头的作用是由谷氨酸能受体介导的。它也对小鼠具有致死性（1.67μg/ g，颅内途径），诱导作用与脑室内给予NMDA报道的相似。 Ap1a（1μM）不会改变乙酰胆碱对横纹肌肉瘤细胞制备的反应，并且对hNa _v1.2，hNa_v1.4，hNa_v1.5和hNa_v1.6通道没有明显影响。由于其独特的序列和半胱氨酸分配给HWTX-II家族，Ap1a对该毒素家族的结构功能研究做出了重要贡献。

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