ABSTRACT
All the 600 living species of cone snails have a highly sophisticated venom production apparatus and delivery system. The venom gland that runs along the foregut synthesizes and secretes the conotoxins (conopeptides). These toxins are small, 15-40 amino acids long, and consist of a conserved core pattern with a highly variable region that is responsible for the multitude of effects conotoxins have. All such toxins are grouped together to form a venom. Most of the conotoxins are the usual paralyzing neurotoxins, but there are some with wider effects, such as sleep inducers. The conus species use their venoms for multiple purposes, including prey capture and defense. Each of these species can produce 50-200 different conotoxins (or ‘conopeptides’) and all such toxins are species-specific (Terlau & Olivera, 2004). Coinciding with their characterization, synthesis
and bioengineering, these peptides have operated as pharmacological probes to dissect ion channel and receptor functions since the 1970s and have now transitioned into analgesic pharmaceuticals (https://www.dehs.umn.edu/ PDFs/Conotoxins.pdf). However, in contrast to the impressive progress made in understanding the toxicology and ecology of cone snails, very few studies have been performed on the venoms of Terebridae and Turridae.
