Erranticosa gen. nov.: a New Genus of Wolf Spiders from East Asia with Notes on its Separation from Lycosa and Hogna (Araneae Lycosidae: Lycosinae)

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  Erranticosa gen. nov.: a New Genus of Wolf Spiders from East Asia with Notes on its Separation from Lycosa and Hogna (Araneae Lycosidae: Lycosinae) Abstract The taxonomy and systematic position of the Eastern Asian wolf spider Lycosa coelestis L. Koch, 1878 are revised using an integrative approach. Our study highlights distinctive morphological and molecular differences that separate this species from the generotypes of Lycosa Sundevall,1833 and Hogna Simon, 1885, to which L. coelestis was previously assigned. Based on these findings, we establish a new monotypic genus, Erranticosa gen. nov., to accommodate this species, namely E. coelestis comb. nov. We also discuss the results of a preliminary molecular phylogenetic analysis of the subfamily Lycosinae, including Erranticosa gen. nov. Additionally, based on morphological examination of the type material, we reject the synonymy of Lycosa subcoelestis Fox, 1935 with E. coelestis comb. nov., transferring it to Trochosa C.L. Koch, ...

Unveiling new Kv1.3 channel blockers from scorpion venom: Characterization of Meuk7–3 and in silico design of its analogs for enhanced affinity and therapeutic potential

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Unveiling new Kv1.3 channel blockers from scorpion venom: Characterization of Meuk7–3 and in silico design of its analogs for enhanced affinity and therapeutic potential

Abstract

Kv1.3 channels are associated with autoimmune and neuroinflammatory diseases. Scorpion venom is an excellent source of inhibitors for Kv1.3. Kv1.3, a pivotal voltage-gated potassium channel, has emerged as a critical therapeutic target for combating autoimmune and neuroinflammatory diseases, including multiple sclerosis and rheumatoid arthritis. Some studies have tried to discover highly selective toxins targeting Kv1.3 channels, but it is still challenging. Here, we present a groundbreaking discovery of a potent peptide potassium channel blocker, Meuk7–3, derived from the venom of the scorpion, Mesobuthus crucittii. While similar to other Kv1.3 blockers, Meuk7–3's Lys19 residue may enhance its affinity for the channel. So, we redesigned the Meuk7–3 and generated three analogous, Meuk7–3 A, Meuk7–3B, and Meuk7–3C, to improve its drug-like properties and affinity to Kv1.3. Interaction evaluation with Kv1.3 revealed that Meuk7–3 and all its designed analogous could of Kv1.3's pore through the interaction of Lys19 of the peptide with Tyr447, Tyr797, Tyr1147, and Tyr1497, critical residues located at the channel pore of Kv1.3.However, the stability of the interaction of designed peptides with Kv1.3 was more than Meuk7–3. Binding affinity analysis revealed that all designed peptides had a better binding affinity to Kv1.3 than Meuk7–3. Among the three analogous, Meuk7–3 A was found to have better drug-like properties and interaction situations, including binding energy and affinity to Kv1.3, compared to Meuk-3 native. These findings provide new data for designing highly effective Kv1.3 inhibitors by computational tools for treating autoimmune and inflammatory diseases, although experimental testing is necessary to validate them.
Shariati, S., Mafakher, L., Shirani, M., & Baradaran, M. (2025). Unveiling new Kv1.3 channel blockers from scorpion venom: Characterization of Meuk7–3 and in silico design of its analogs for enhanced affinity and therapeutic potential. International Journal of Biological Macromolecules, 319, 145327. https://doi.org/10.1016/j.ijbiomac.2025.145327