Extreme diversity of scorpion venom peptides and proteins revealed by transcriptomic analysis: Implication for proteome evolution of scorpion venom arsenal

Variability of Potassium Channel Blockers in Mesobuthus eupeus Scorpion Venom with Focus on Kv1.1

“…For several scorpion species such studies were carried out and a large variety of peptides and proteins were thus predicted (54 -56). This set includes not only active venom components (such as ion channel toxins, cytolytic peptides, and enzymes) but also housekeeping proteins, some of which are responsible for cellular metabolism (29). Of course, the main target of such studies is different bioactive molecules and, in particular, toxins interacting with potassium and sodium channels.…”

“…The purified individual compounds are then subjected to protein sequencing. More recently, venom gland transcriptomics was introduced to aid high throughput sequencing of scorpion toxins (27)(28)(29). The recovered sequence information from a transcriptome database is then analyzed based on identified similarities with the already known toxins.…”

Unique diversity of the venom peptides from the scorpion Androctonus bicolor revealed by transcriptomic and proteomic analysis

“…The transcripts of NaTxs and KTxs are largely dominant, accounting for 36.9% of the total venom peptide transcripts of A. bicolor. This expression level is higher than those of Tityus stigmurus (14.8%), L. mucronatus (21.8%), and Isometrus maculatus (17.5%), but is lower than that of Centruroides noxius (54.6%), one of the most poisonous scorpions in the world [17,25,32]. It was shown that the sting of A. bicolor may cause pain, hyperemia, vomiting, swelling, restlessness and hypotension [73].…”

“…The five peptides are rich in the basic amino acid residues Arg and Lys, which account for 39.6%-37.3% of the total residues, respectively; this makes them highly hydrophilic and basic, having very high isoelectric points (12.18-12.31). BLAST search against the GenBank database revealed that AbTxC 2 1, AbTxC 2 2, AbTxC 2 3, AbTxC 2 4 and AbTxC 2 5 showed 48%-44% sequence identities with VP1.1 and VP27.1 from the scorpion L. mucronatus [25,36], respectively (Fig. 12A).…”

Discoveries of Serine Protease Inhibitors from Scorpions

“…Here, in this review, we report updated information about the protease inhibitors described to date from scorpions. pressure, scorpions produce more efficient toxic peptides / proteins to be evolutionarily successful [32][33][34]. Suggestively, these peptides / proteins act as protease inhibitors to protect their venom peptides from degradation.…”