Two new arthropod toxins purified from the venom of the Mexican scorpion Centruroides nigrescens

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  Two new arthropod toxins purified from the venom of the Mexican scorpion Centruroides nigrescens Abstract The venom of the slender black scorpion Centruroides nigrescens , from the State of Guerrero México, was fractionated by Sephadex G–50 gel filtration, followed by carboxymethyl cellulose ion separation and high–performance liquid chromatography, permitting to obtain two new peptides toxic to arthropods. The estimate LD 50 of the soluble venom for the insect Acheta domesticus was 11.1 μg/g body weight, and for the arthropod Armadillidium vulgare was 61.1 μg body weight . The amino acid sequence of toxin Cnige1 (toxic to A. domesticus and A. vulgare ) contains 65 amino acids, with a molecular mass of 7273.37 mass units, whereas toxin Cnige2, toxic to A. domesticus , contains 68 amino acids, with a molecular mass of 7548.81 units. Both peptides are well packed, containing 8 cysteines, which in the native venoms are forming 4 disulfide bridges each. The amino acid sequences f...

Divergence in toxin antigenicity and venom enzymes in Tityus melici, a medically important scorpion, despite transcriptomic and phylogenetic affinity with problematic Brazilian species

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Divergence in toxin antigenicity and venom enzymes in Tityus melici, a medically important scorpion, despite transcriptomic and phylogenetic affinity with problematic Brazilian species

Abstract

The Brazilian scorpion Tityus melici, native to Minas Gerais and Bahia, is morphologically related to Tityus serrulatus, the most medically significant species in Brazil. Despite inhabiting scorpion-envenomation endemic regions, T. melici venom remains unexplored. This work evaluates T. melici venom composition and function using transcriptomics, enzymatic activities, and in vivo and in vitro immunological analyses. Next-Generation Sequencing unveiled 86 components putatively involved in venom toxicity: 39 toxins, 28 metalloproteases, seven disulfide isomerases, six hyaluronidases, three phospholipases and three amidating enzymes. T. serrulatus showed the highest number of toxin matches with 80–100 % sequence similarity. T. melici is of medical importance as it has a venom LD50 of 0.85 mg/kg in mice. We demonstrated venom phospholipase A2 activity, and elevated hyaluronidase and metalloprotease activities compared to T. serrulatus, paralleling our transcriptomic findings. Comparison of transcriptional levels for T. serrulatus and T. melici venom metalloenzymes suggests species-specific expression patterns in Tityus. Despite close phylogenetic association with T. serrulatus inferred from COI sequences and toxin similarities, partial neutralization of T. melici venom toxicity was achieved when using the anti-T. serrulatus antivenom, implying antigenic divergence among their toxins. We suggest that the Brazilian therapeutic scorpion antivenom could be improved to effectively neutralize T. melici venom.


Kalapothakis, Y., Miranda, K., Aragão, M., Larangote, D., Braga-Pereira, G., Noetzold, M., Molina, D., Langer, R., Conceição, I. M., Guerra-Duarte, C., Chávez-Olórtegui, C., Kalapothakis, E., & Borges, A. (2024). Divergence in toxin antigenicity and venom enzymes in Tityus melici, a medically important scorpion, despite transcriptomic and phylogenetic affinity with problematic Brazilian species. International Journal of Biological Macromolecules, 130311. https://doi.org/10.1016/j.ijbiomac.2024.130311