A rare complication of scorpion venom: atrial fibrillation

Duman, Ali; Türkdoğan, Kenan Ahmet; Aköz, Ayhan; Avcil, Mücahit; Dağlı, Bekir; Çanakçı, Selçuk Eren

doi:10.1016/j.ajem.2015.09.046

Cited by 1 publication

(1 citation statement)

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“…The venom of Buthidae scorpions is rich in neurotoxins acting on voltage-dependent ion channels that are responsible for symptomatologic signs in autonomic hyperactivity (tachycardia, hypertension, cardiac arrhythmias, mydriasis, excessive salivation and tearing, bradycardia, hypotension, and others) [ 4 , 37 , 38 ]. When these accidents occur, they might cause death, as a consequence of cardiovascular defects attributed to the massive release of catecholamines from the adrenal glands and noradrenergic nerve terminals, together with complications associated with pulmonary edema and respiratory failure in mammals [ 4 , 39 , 40 ].…”

Section: Discussionmentioning

confidence: 99%

Colombian Scorpion Centruroides margaritatus: Purification and Characterization of a Gamma Potassium Toxin with Full-Block Activity on the hERG1 Channel

Beltrán-Vidal

Carcamo-Noriega

Pastor

et al. 2021

Toxins

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The Colombian scorpion Centruroides margaritatus 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 humanether-à-go-go-Related 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 Centruroides margaritatus 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 IC50 of 3.4 ± 0.2 nM. Despite its 90.5% identity with toxin ɣ-KTx1.1, isolated from Centruroides noxius, CmERG1 completely blocks hERG1 current, suggesting a more stable plug of the hERG channel, compared to that formed by other ɣ-KTx.

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