Spider venom peptides Ht1a and Gg1a are toxic to honeybee parasite Varroa destructor by topical application

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  Spider venom peptides Ht1a and Gg1a are toxic to honeybee parasite Varroa destructor by topical application Abstract Global food supply strongly depends on honeybee pollination services, which are threatened by insecticides and pests such as parasitic Varroa destructor mites. Chemical varroacides/acaricides are hampered by resistance development, necessitating the development of sustainable and environmentally friendly alternatives, with arthropod venom peptides being considered promising sources of acaricidal toxins. With only a few acaricidal venom peptides being reported, we performed a systematic topical screening of 50 arthropod venoms against V. destructor , with 78% of the venoms causing 100% mortality after 24 h. Deconvolution of the venoms from the Tasmanian cave spider Hickmania troglodytes and the Giant Japanese funnel-web spider Gigathele gigas led to identification of the varroacidal peptides Ht1a and Gg1a. Topical application of Ht1a and Gg1a reduced varroa mite ...

Functional and immunological variability of Viperid venoms across continents and cross-neutralization by Peruvian antivenoms

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By Holger Krisp - Own work, CC BY 3.0, https://commons.wikimedia.org/w/index.php?curid=75251850

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., Yarlequé, A., & Vivas-Ruiz, D. E. (2026). Functional and immunological variability of Viperid venoms across continents and cross-neutralization by Peruvian antivenoms. Biochimie, 240, 88-99. https://doi.org/10.1016/j.biochi.2025.10.013