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 ...

Transcriptomic and Proteomic Analyses Reveals the Diverse Venom Composition of the Spider Neoscona shillongensis

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Transcriptomic and Proteomic Analyses Reveals the Diverse Venom Composition of the Spider Neoscona shillongensis

Abstract

Neoscona shillongensis (Araneidae), also known as the Shillong orb-weaving spider, is a species that constructs a typically shaped round web, is inactive during the daytime and comes out at dusk to forage, primarily preying on flying insects such as mosquitoes, flies, and moths. This spider serves as an important natural enemy of agricultural and forest pests. Neoscona shillongensis primarily uses its web to capture prey, but its venom also plays a crucial role in subduing and processing prey. To date, no research has been conducted on the composition of N. shillongensis venom. In This study, conducted high-throughput sequencing on the venom gland transcriptome and the venom gland extract proteome. A cDNA library of the venom gland tissue of N. shillongensis was constructed, yielding over 62 million reads, which were assembled into 90,481 sequences, predicting 171 toxin-like sequences, including 94 peptide toxins and 77 protein toxins. Furthermore, proteomic analyses of the venom gland extract samples identified 53 peptides and proteins, including 23 peptide toxins and 30 enzymes or proteins such as acetylcholinesterase, hyaluronidase, and astacin-like metalloproteases. The results revealed that the toxin composition of N. shillongensis is diverse and complex. This study provides essential baseline data for further research on the evolution and physiological activity of spider venom, as well as the potential development of pharmaceutical compounds therefrom.
Yin, W., You, Y., Tembrock, L. R., Zhang, M., Li, Z., Zheng, Y., Yu, Z., & Yang, Z. (2025). Transcriptomic and Proteomic Analyses Reveals the Diverse Venom Composition of the Spider Neoscona shillongensis. Insect Biochemistry and Molecular Biology, 104289. https://doi.org/10.1016/j.ibmb.2025.104289