Clinical characteristics and long-term disabilities in children following Bothrops atrox envenomation in Manaus, western Brazilian Amazon

  Image Credit: By Darío De la Fuente - https://www.inaturalist.org/photos/113840233, CC BY 4.0, https://commons.wikimedia.org/w/index.php?curid=129474300 Clinical characteristics and long-term disabilities in children following Bothrops atrox envenomation in Manaus, western Brazilian Amazon Abstract Background:   In the Brazilian Amazon, most snakebites are caused by Bothrops atrox . Although pediatric cases are less frequent, children are more vulnerable to severe complications and long-term disabilities. This study aims to describe the clinical profile of B. atrox envenomation in children treated at a tertiary hospital in Manaus, in Western Brazilian Amazon, and to characterize the resulting long-term musculoskeletal impairments in a subgroup of these patients. Methods:   We retrospectively analyzed sociodemographic and clinical data from patients up to 12 years and 11 months of age treated between January 2010 and December 2023. A total of 258 children who were ...

Cvill6 and Cvill7: Potent and Selective Peptide Blockers of Kv1.2 Ion Channel Isolated from Mexican Scorpion Centruroides villegasi

 


Cvill6 and Cvill7: Potent and Selective Peptide Blockers of Kv1.2 Ion Channel Isolated from Mexican Scorpion Centruroides villegasi

Abstract

Scorpion venoms are a rich source of peptides that modulate the activity of ion channels and can serve as a new drug for channelopathies. Cvill6 and Cvill7 are two new peptides isolated from the venom of Centruroides villegasi with MW of 4277 Da and 4287 Da and they consist of 38 and 39 amino acids, respectively, including six cysteines. Sequence alignment revealed high similarity with members of the α-KTx2 subfamily of potassium channel toxins. In electrophysiology, Cvill7 potently inhibited Kv1.2 ion channels with an IC50 of 16 pM and Kv1.3 with an IC50 of 7.2 nM. In addition, it exhibited partial activity on KCa3.1 and Kv1.1, with ~16% and ~34% inhibition at 100 nM, respectively. In contrast, Cvill6 blocked Kv1.2 with low affinity (IC50 of 3.9 nM) and showed modest inhibition of Kv1.3 (~11%) and KCa3.1 (~27%) at 100 nM concentration. Neither peptide showed any activity against other K+ channels tested in this study (Kv1.5, Kv11.1, KCa1.1, and KCa2.2). Notably, Cvill7 has a remarkable affinity for Kv1.2 and high selectivity of 450-fold over Kv1.3 and 12,000-fold over Kv1.1. These pharmacological properties make Cvill7 a potential candidate to target Kv1.2 gain of function (GOF)-related channelopathies such as epilepsy.

Shakeel, K., Naseem, M. U., Zamudio, F. Z., Possani, L. D., & Panyi, G. (2025). Cvill6 and Cvill7: Potent and Selective Peptide Blockers of Kv1.2 Ion Channel Isolated from Mexican Scorpion Centruroides villegasi. Toxins, 17(6), 279. https://doi.org/10.3390/toxins17060279