Qualitative and Quantitative Proteomic Analysis of Venoms from Mexican Rattlesnakes

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  Qualitative and Quantitative Proteomic Analysis of Venoms from Mexican Rattlesnakes Abstract Despite the vast biodiversity of Mexican vipers, venom of endemic species has been barely studied. Here we analyzed the venom composition of three endemic species of rattlesnakes: Crotalus aquilus , C. triseriatus , and C. ravus . We used quantitative chromato-mass-spectrometry and compared venoms with C. molossus , a species commonly found in North America, in a comparative and phylogenetic framework. In total, we identified 165 proteins grouped in 19 main protein families, consistent with previous reports for viperid venoms. In C. aquilus and C. triseriatus , the most predominant protein-family type was Serine Proteases, and in C. triseriatus and C. molossus it was Snake Venom Metalloproteases. The Label-free quantification revealed a high proportion of Snake Venom Metalloproteases in C. aquilus , C. triseriatus , and C. molossus , reaching 28–47% of the total venom. In contrast, in ...

Functional and Immunological Variability of Viperid Venoms Across Continents and Cross-Neutralization by Peruvian Antivenoms

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Functional and Immunological Variability of Viperid Venoms Across Continents and Cross-Neutralization by Peruvian Antivenoms

Abstract

Snake envenomation remains a significant neglected tropical disease primarily treated with antivenoms, which, despite inherent limitations, continue to be the gold standard therapy. Snake venoms exhibit extensive compositional and functional diversity, posing challenges for universal antivenom efficacy. This study comprehensively evaluated venom composition, enzymatic activities, and immunological cross-reactivity across 24 Viperidae species from diverse geographic regions. Using protein profiling, enzymatic assays (proteolytic, amidolytic, clotting, and PLA2 activities), and phylogenetic analyses, we revealed marked interspecific variation. Bothrops species exhibited elevated SVMP-driven proteolytic activity, while Crotalus venoms demonstrated more balanced enzymatic profiles. Phylogenetic clustering highlighted evolutionary divergence and functional convergence among taxa. Immunoreactivity assays with Peruvian antibothropic, anticrotalic, and antilachesic antivenoms showed broad cross-recognition within Bothrops and Crotalus venoms, but limited efficacy against more distantly related Viperinae species. Western blot analyses confirmed these specificity patterns. Neutralization assays revealed differential inhibition: antibothropic antivenom effectively neutralized proteolytic activity, whereas anticrotalic antivenom preferentially inhibited PLA2-mediated effects. This functional variability highlights the biochemical complexity of viperid venoms and the constraints of current antivenoms. Our findings emphasize the urgent need to develop improved, broadly effective antivenom formulations capable of targeting the diverse toxin profiles of geographically and phylogenetically distinct viperid species, ultimately enhancing clinical management of snakebite envenomation worldwide.
Torrejón, D., Llontop, A., Proléon, A., Lazo, F., Urra, F. A., Yarlequé, A., & Vivas-Ruiz, D. E. (2025). Functional and Immunological Variability of Viperid Venoms Across Continents and Cross-Neutralization by Peruvian Antivenoms. Biochimie. https://doi.org/10.1016/j.biochi.2025.10.013