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 ...

Integrative transcriptomic and proteomic analysis reveals the toxin diversity of the spider Macrothele bannaensis

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Integrative transcriptomic and proteomic analysis reveals the toxin diversity of the spider Macrothele bannaensis

Abstract

Spider toxins are an important and abundant source of bioactive compounds and represent molecular candidates for the development of novel compounds for use in medicine and agriculture. Despite the vast diversity of spider species, only a small fraction of them have been studied in detail regarding venom chemistry. Macrothele bannaensis, a spider belonging to the family Macrotheleidae, is widely distributed in the Xishuangbanna region of Yunnan, China, and serves as an important natural enemy of agricultural pests. However, there is a lack of research on the composition of its venom. In this study, the venom composition of M. bannaensis was outlined for the first time through the joint analysis of venom gland transcriptomics and venom proteomics. A total of 65 toxin sequences were identified in the venom gland transcriptome, including 23 typical DRPs (Disulfide-rich peptides), which were categorized into 11 superfamilies based on the arrangement of cysteines. In addition, other proteins, such as CRISPs (cysteine-rich secretory proteins), acetylcholinesterase, and hyaluronidase, were also identified. Proteomic analysis identified 35 components, including 12 DRPs, 23 enzymes and other functional proteins. This study systematically elucidated the molecular diversity of toxins in M. bannaensis, providing an important resource for better understanding the biology of this spider and for the discovery of new therapeutic and agricultural compounds.
Zheng, Y., Yin, W., Tembrock, L. R., Yang, M., Zhang, M., Zhao, Y., & Yang, Z. (2025). Integrative transcriptomic and proteomic analysis reveals the toxin diversity of the spider Macrothele bannaensis. International Journal of Biological Macromolecules, 322, 146740. https://doi.org/10.1016/j.ijbiomac.2025.146740