Studying the venom composition of scorpions is important. It is important to know the venom composition in medical important species to understand their pathological effect and better be able to develop antivenom or treatment. In addition, scorpion venom is a treasure chest filled with different peptides and toxins that can be used to develop medicines.
Karla Bordon and co-workers recently published a study presenting a comprehensive biochemical characterization of venom from three Amazonian species, Tityus metuendus Pocock, 1897, T. silvestris Pocock, 1897 (both Buthidae) and Brotheas amazonicus Lourenço, 1988 (Chactidae).
According to the article, "the results suggest a correlation between ecological divergence and venom composition, with implications for both toxicity and antivenom development".
Abstract:
Scorpionism is a growing public health concern in Brazil, with the Amazon region presenting the highest mortality rates but remaining understudied, especially regarding local scorpion venoms composition. This study presents the first comprehensive biochemical characterization of venoms from three Amazonian species—Tityus metuendus (TmetuV), Tityus silvestris (TsilvV), and Brotheas amazonicus (BamazV)—using an integrated approach combining Multi-Enzymatic Limited Digestion (MELD)-based bottom-up proteomics, highresolution LC-MS/MS, chromatography, zymography, and enzymatic assays. Tityus serrulatus venom was included as a reference. Significant biochemical differences were observed: TsilvV was rich in 20–30 kDa proteins and showed strong metalloprotease activity; BamazV exhibited high molecular weight proteins and potent phospholipase A2 (PLA2)
activity but lacked proteolytic and fibrinogenolytic activities; TmetuV showed the highest hyaluronidase activity and abundance of α-KTx neurotoxins. Zymography revealed a conserved ~45 kDa hyaluronidase in all species. Three novel components were partially characterized: BamazPLA2 (Group III PLA2), Tmetu1 (37-residue α-KTx), and TsilvMP_A (a metalloprotease homologous to antarease). This is the first application of MELD-based proteomics to Amazonian scorpion venoms, revealing molecular diversity and functional divergence within Tityus and Brotheas, emphasizing the need for region-specific antivenoms. These findings provide a foundation for future pharmacological studies and the discovery of bioactive peptides with therapeutic potential.
Reference:
Bordon KC, Santos GC, Martins JG, Wiezel GA, Amorim FG, Crasset T, et al. Pioneering Comparative Proteomic and Enzymatic Profiling of Amazonian Scorpion Venoms Enables the Isolation of Their First α-Ktx, Metalloprotease, and Phospholipase A2. Toxins. 2025;17(8):411. [Open Access]
Thanks to Jonas Martins for sending me their article!
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