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...

Novel Biochemical Findings from Bothrops marajoensis Venom

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Novel Biochemical Findings from Bothrops marajoensis Venom

Abstract

Bothrops marajoensis is a Brazilian pit viper whose venom remains poorly characterized compared with those of other medically important Bothrops species. In the present study, we performed a comparative biochemical characterization of B. marajoensis venom with six additional Bothrops venoms (B. alternatus, B. atrox, B. jararaca, B. jararacussu, B. moojeni, and B. neuwiedi). Venoms were analyzed by reversed-phase chromatography, electrophoresis, immunorecognition by commercial bothropic antivenom, phosphodiesterase activity, and their effects on the viability of differentiated C2C12 myotubes. Chromatographic and electrophoretic analyses revealed a largely conserved overall venom composition among species, with qualitative differences, although quantitative differences in protein relative abundance were evident. Bothropic antivenom recognized all venoms, indicating broad antigenic cross-reactivity despite venom variation. B. marajoensis exhibited intermediate phosphodiesterase (PDE) activity relative to other species evaluated, confirming functional variability among Bothrops venoms. In the cell viability assay, B. marajoensis displayed comparatively low apparent cytotoxicity toward differentiated C2C12 myotubes, maintaining higher cell viability than highly myotoxic venoms such as those of B. jararacussu and B. moojeni. These findings expand the biochemical characterization of B. marajoensis venom and demonstrate that, although venoms share the conserved toxin repertoire typical for Bothrops genus, quantitative differences influence its biological activities, preserving broad recognition by bothropic antivenom.

Oliveira, I., Ferreira, I., Jacob, B., Ramos, E., Agati, L., Lino, I., Cordeiro, F., Costa, F., Filardi, E., Pucca, M., & Arantes, E. (2026). Novel Biochemical Findings from Bothrops marajoensis Venom. International Journal of Molecular Sciences, 27(19), 8524. https://doi.org/10.3390/ijms27198524