Analysis of the Proteome and Biochemistry of Venom from , a Scorpion That Can Be Involved in Severe Envenomation Cases in Brazil.

In Brazil, the annual scorpion sting cases surpass those of other neglected tropical diseases, highlighting a significant public health issue. The severity of scorpion envenomation relates to the venom's rapid action, complex composition, species identification challenges, and limited antivenom availability. This work aimed to characterize the venom of through proteomic, enzymatic, and biological analyses while also assessing its reactivity to anti-scorpion antivenom. The electrophoretic analysis revealed seven protein bands, with the most prominent bands at 30, 15, and 10 kDa. The C18-RP-HPLC analysis isolated sixteen primary fractions. The proteomic analysis identified various toxins, including potassium channel toxins, sodium channel toxins, and antimicrobial peptides, as well as other proteins such as hypotensin and metalloproteinases. Antigenic components were identified in the . venom, which displayed dose-dependent but time-independent amylolytic activity. The ATPase activity significantly increased with 1-10 μg of venom. No cytotoxic effects were observed on carcinoma or non-tumoral cell lines. The . venom features a complex protein composition rich in toxins that target ion channels and enzymes. It exhibits active enzymatic and antigenic properties, and displays low cytotoxicity. This is the first proteomic research on the composition of . venom and may provide valuable insights into understanding the clinical manifestations of scorpion stings.