Venomics of the six-eyed sand spider, Sicarius rugosus (Araneae: Sicariidae), from the neotropical dry forest of Costa Rica

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  Venomics of the six-eyed sand spider, Sicarius rugosus (Araneae: Sicariidae), from the neotropical dry forest of Costa Rica Abstract Background Sicarius rugosus , the only member of the genus that inhabits Central America, is phylogenetically related to South American  Sicarius  spiders. These originated from a common ancestor with sister African species. Like  Loxosceles ,  Sicarius  exhibits venom phospholipase D activity due to a group of toxins known collectively as SicTox. Methods A gel-assisted, bottom-up, proteomic analysis was performed to characterize the venom composition of  S. rugosus . Hyaluronidase activity was determined using zymography. Results We identified several SicTox sequences, all classified as β-clade paralogs and sharing unique peptides with proteins from  S. patagonicus ,  S. peruensis,  and other species. Enzymes such as metalloproteinases, including putative astacins, carboxypeptidases, and angiotensin-conv...

Crotoxin B from the South American Rattlesnake Crotalus vegrandis Blocks Voltage-Gated Calcium Channels Independent of Its Intrinsic Catalytic Activity

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By Patrick JEAN / muséum d'histoire naturelle de Nantes - Muséum d'histoire naturelle de Nantes (archive copy at the Wayback Machine), Copyrighted free use, https://commons.wikimedia.org/w/index.php?curid=29697

Crotoxin B from the South American Rattlesnake Crotalus vegrandis Blocks Voltage-Gated Calcium Channels Independent of Its Intrinsic Catalytic Activity

Abstract

Neurotoxicity following South American Crotalus rattlesnake bite is primarily caused by crotoxin, the most abundant component in their venom. Despite the central role of voltage-gated calcium channels (CaV) in neurotransmission, direct targetability by crotoxin has been poorly explored. Crotoxin is a non-covalent heterodimer formed by an acidic subunit (CA) and a basic toxic phospholipase A2 subunit (CB). Here, we chromatographically isolated the CB subunit from Crotalus vegrandis and studied its effect on CaV heterologously expressed in tsA201 cells using the whole-cell patch-clamp technique. Mass spectrometry analysis identified a protein that matched with 97% sequence coverage the CBc isoform from Crotalus durissus terrificus. Isolated CB exhibited moderate phospholipase activity that was not correlated to its cytotoxic effect on cultured tsA201 cells. Using Ba2+ as a charge carrier to prevent the enzymatic activity, we found that CB inhibited currents mediated by the N-type CaV2.2 and CaV1.2 L-type calcium channels, in a dose–dependent manner, with higher potency for the latter, and negligible changes in the voltage dependence of channel activation. Our results reveal a novel phospholipase-independent biological activity and a molecular target of CB providing new insights into the pathophysiology of Crotalus snakebite envenoming with potential clinical therapeutic implications.

Eicheldinger, M., Castilla, F., Jordan, N., & Hidalgo, P. (2026). Crotoxin B from the South American Rattlesnake Crotalus vegrandis Blocks Voltage-Gated Calcium Channels Independent of Its Intrinsic Catalytic Activity. Toxins, 18(1), 36. https://doi.org/10.3390/toxins18010036