Mass-Spectrometry-Based Lipidome and Proteome Profiling of Hottentotta saulcyi (Scorpiones: Buthidae) Venom

Scorpion venom is a complex secretory mixture of components with potential biological and physiological properties that attracted many researchers due to promising applications from clinical and pharmacological perspectives. In this study, we investigated the venom of the Iranian scorpion Hottentotta saulcyi (Simon, 1880) by applying mass-spectrometry-based proteomic and lipidomic approaches to assess the diversity of components present in the venom. The data revealed that the venom's proteome composition is largely dominated by Na⁺- and K⁺-channel-impairing toxic peptides, following the enzymatic and non-enzymatic protein families, e.g., angiotensin-converting enzyme, serine protease, metalloprotease, hyaluronidase, carboxypeptidase, and cysteine-rich secretory peptide. Furthermore, lipids comprise ~1.2% of the dry weight of the crude venom. Phospholipids, ether-phospholipids, oxidized-phospholipids, triacylglycerol, cardiolipins, very-long-chain sphingomyelins, and ceramides were the most intensely detected lipid species in the scorpion venom, may acting either independently or synergistically during the envenomation alongside proteins and peptides. The results provide detailed information on the chemical makeup of the venom, helping to improve our understanding of biological molecules present in it, leading to a better insight of the medical significance of the venom, and improving the medical care of patients suffering from scorpion accidents in the relevant regions such as Iran, Iraq, Turkey, and Afghanistan.