Grupo de Investigaciones Herpetológicas y Toxinológicas, Centro de Investigaciones Biomédicas, Departamento de Biología, Facultad de Ciencias Naturales, Exactas y de la Educación, Universidad del Cauca, Sector Tulcan, Calle 2 N 3N-100, Popayán 190002, Cauca, Colombia.
Grupo de Investigación Laboratorio de Herpetología y Toxinología, Departamento de Fisiología, Facultad de Salud, Universidad del Valle, Calle 4B N° 36-00, Santiago de Cali 760043, Valle del Cauca, Colombia.
Toxins (Basel). 2021 Jun 8;13(6):407. doi: 10.3390/toxins13060407.
The Colombian scorpion produces a venom considered of low toxicity. Nevertheless, there are known cases of envenomation resulting in cardiovascular disorders, probably due to venom components that target ion channels. Among them, the gene (hERG1) potassium channels are critical for cardiac action potential repolarization and alteration in its functionality are associated with cardiac disorders. This work describes the purification and electrophysiological characterization of a venom component acting on hERG1 channels, the CmERG1 toxin. This novel peptide is composed of 42 amino acids with a MW of 4792.88 Da, folded by four disulfide bonds and it is classified as member number 10 of the γ-KTx1 toxin family. CmERG1 inhibits hERG1 currents with an IC of 3.4 ± 0.2 nM. Despite its 90.5% identity with toxin ɣ-KTx1.1, isolated from , CmERG1 completely blocks hERG1 current, suggesting a more stable plug of the hERG channel, compared to that formed by other ɣ-KTx.
哥伦比亚蝎子产生的毒液被认为毒性较低。然而，已知有一些因蝎子蜇伤导致心血管疾病的病例，这可能是由于毒液成分靶向离子通道。其中， 基因（hERG1）钾通道对于心脏动作电位复极化至关重要，其功能的改变与心脏疾病有关。本工作描述了一种作用于 hERG1 通道的 毒液成分的纯化和电生理特性，即 CmERG1 毒素。这种新型肽由 42 个氨基酸组成，MW 为 4792.88 Da，由四个二硫键折叠而成，被归类为 γ-KTx1 毒素家族的第 10 个成员。CmERG1 以 3.4 ± 0.2 nM 的 IC 抑制 hERG1 电流。尽管它与从 中分离得到的毒素 ɣ-KTx1.1 具有 90.5%的同一性，但 CmERG1 完全阻断 hERG1 电流，这表明与其他 ɣ-KTx 形成的通道相比，它形成了更稳定的 hERG 通道塞子。
