In Memoriam: Gérard Dupré (1947–2026) — A Life Devoted to the Study of Scorpions

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  Photo Credit: Le Parisien In Memoriam: Gérard Dupré (1947–2026) — A Life Devoted to the Study of Scorpions The passing of Gérard Dupré (1947–2026) is a deeply felt loss for those of us who share an interest in the study of scorpions and other arachnids. Throughout his life, he dedicated himself to documenting and preserving arachnological knowledge, contributing valuable work on scorpion taxonomy, distribution, and bibliography. His careful attention to the literature helped bring clarity and organization to a field whose history spans centuries and many languages. Gérard was also closely associated with the journal Arachnides , which became an important outlet for sharing research, faunistic records, and historical notes within the arachnological community. Through this work, he helped ensure that observations and studies—large and small—were preserved and made accessible to others with similar scientific interests. Beyond his scholarly contributions, Gérard was a humble and gen...

Molecular diversity of peptides from Pandercetes sp. spider venom and antagonistic activity on voltage-gated calcium channels of the κ-LhTx-1 toxin

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Molecular diversity of peptides from Pandercetes sp. spider venom and antagonistic activity on voltage-gated calcium channels of the κ-LhTx-1 toxin

Abstract

The venom of toxic animals represents a rich reservoir of bioactive peptides, which serve as invaluable tools for ion channel research, drug and insecticide development. While venoms of various species have been extensively studied, the venom composition of spiders from the Pandercetes genus remains largely unexplored. In this study, the peptide diversity of spider Pandercetes sp. was explored by constructing a venom cDNA library. A total of 626 high-quality expression sequence tags (ESTs) were obtained, categorized into toxin-like ESTs, cellular component ESTs, and non-classified ESTs. From the toxin-like ESTs, 102 non-redundant toxin-like peptides were identified and grouped into 11 families according to sequence homology and cysteine framework. Bioinformatic analysis revealed these peptide toxins share moderate similarity with those identified in the venoms of Heteropoda pingtungensis and Heteropoda venatoria. Mass spectrometric analysis identified 154 peptides with molecular masses ranging from 1000 to 8000 Da, underscoring the diverse and intricate nature of the venom. However, the biological functions of the major toxins remain largely unknown. To address this, venom fractions obtained by reverse-phase high-performance liquid chromatography (RP-HPLC) were assessed for inhibition of voltage-gated calcium channel currents using patch-clamp electrophysiology. Notably, κ-LhTx-1, a highly abundant peptide, was previously identified as a selective inhibitor of mammalian Kv4 channels, and also exhibits inhibitory activity against L-type Cav channels, reflecting its multi-target role. In conclusion, this study provides a novel insight into the molecular diversity in the venoms of spider Pandercetes sp. and lays a foundation for the discovery of active molecules.
Tang, D., You, Q., Hu, Z., He, Y., Yi, Y., Chang, J., Wang, C., Tang, C., Du, S., & Xiao, Z. (2026). Molecular diversity of peptides from Pandercetes sp. Spider venom and antagonistic activity on voltage-gated calcium channels of the κ-LhTx-1 toxin. International Journal of Biological Macromolecules, 337, 149490. https://doi.org/10.1016/j.ijbiomac.2025.149490