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Envenoming by Macrovipera lebetina subspecies causes severe life-threatening difficulties for people living in North Africa and the Middle East. To better understand the pathophysiology of envenoming and improve patient management, knowledge about the venom components of the subspecies is essential. Here, the venom proteomes of Macrovipera lebetina lebetina from Cyprus and Macrovipera lebetina cernovi from Iran were characterized using RP-HPLC separation of the crude venom proteins, SDS-PAGE of fractionated proteins, and LC-MS/MS of peptides obtained from in-gel tryptic digestion of protein bands. Moreover, we also used high-resolution shot-gun proteomics to gain more reliable identification, where the whole venom proteomes were subjected directly to in-solution digestion before LC-HR-MS/MS. The data revealed that both venoms consisted of at least 18 protein families, of which snake venom Zn2+-dependent metalloprotease (SVMP), serine protease, disintegrin, phospholipase A2, C-type lectin-like, and L-amino acid oxidase, together accounted for more than 80% of the venoms’ protein contents. Although the two viper venoms shared mostly similar protein classes, the relative occurrences of these toxins were different in each snake subspecies. For instance, P-I class of SVMP toxins were found to be more abundant than P-III class in the venoms of M. l. cernovi compared to M. l. lebetina, which gives hints at a more potent myonecrotic effect and minor systemic hemorrhage following envenoming by M. l. cernovi than M. l. lebetina. Moreover, single-shot proteomics also revealed many proteins with low abundance (M. lebetina subspecies, particularly regarding toxin families associated with envenoming pathogenesis and those hard-detected protein classes expressed in trace amounts.

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.

Snakes of the genera Pseudocerastes and Eristicophis (Viperidae: Viperinae) are known as the desert vipers due to their association with the arid environments of the Middle East. These species have received limited research attention and little is known about their venom or ecology. In this study, a comprehensive analysis of desert viper venoms was conducted by visualising the venom proteomes via gel electrophoresis and assessing the crude venoms for their cytotoxic, haemotoxic, and neurotoxic properties. Plasmas sourced from human, toad, and chicken were used as models to assess possible prey-linked venom activity. The venoms demonstrated substantial divergence in composition and bioactivity across all experiments. Pseudocerastes urarachnoides venom activated human coagulation factors X and prothrombin and demonstrated potent procoagulant activity in human, toad, and chicken plasmas, in stark contrast to the potent neurotoxic venom of P. fieldi. The venom of E. macmahonii also induced coagulation, though this did not appear to be via the activation of factor X or prothrombin. The coagulant properties of P. fieldi and P. persicus venoms varied among plasmas, demonstrating strong anticoagulant activity in the amphibian and human plasmas but no significant effect in that of bird. This is conjectured to reflect prey-specific toxin activity, though further ecological studies are required to confirm any dietary associations. This study reinforces the notion that phylogenetic relatedness of snakes cannot readily predict venom protein composition or function. The significant venom variation between these species raises serious concerns regarding antivenom paraspecificity. Future assessment of antivenom is crucial.