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 ...

Serine proteases and serine protease inhibitors identified from the venom gland transcriptome of Rhitymna verruca

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Serine proteases and serine protease inhibitors identified from the venom gland transcriptome of Rhitymna verruca

Abstract

Rhitymna verruca is a large nocturnal wandering spider and an important natural predator of agricultural and forestry pests, with its venom playing a key role in prey capture. However, systematic studies on the composition of its venom remain scarce. In this study, we performed an integrated analysis of the venom gland and venom samples using high-throughput transcriptome sequencing combined with quantitative proteomics. The transcriptome yielded 43,244 representative unigene sequences, among which 102 toxin-like sequences were identified through functional annotation, encompassing 13 peptide toxin superfamilies and 7 protein toxin families. Proteomic analysis identified 35 venom components, including 14 peptide toxins and 21 functional proteins. The most abundantly expressed toxin families, Superfamily IX and VII, were highly expressed at both transcriptomic and proteomic levels, suggesting central roles in prey paralysis and neuroregulation. Most peptide toxins possessed ICK or Kunitz domains, indicating high structural stability and potential target specificity. In addition, the venom was rich in auxiliary components such as CAP protein superfamily, hyaluronidases, and metalloproteases, which may contribute to toxin synergy, diffusion, and tissue disruption. This study provides the first comprehensive characterization of the venom composition of R. verruca, offering fundamental insights into its functional mechanisms, evolutionary patterns, and potential applications in the development of novel bioactive agents.
Li, Z., Zhang, M., Yin, W., Zheng, Y., Liu, H., Zhao, Y., & Yang, Z. (2026). Serine proteases and serine protease inhibitors identified from the venom gland transcriptome of Rhitymna verruca. Comparative Biochemistry and Physiology Part D: Genomics and Proteomics, 58, 101719. https://doi.org/10.1016/j.cbd.2025.101719