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Comment published on 15 January 2026, see Toxins 2026, 18(1), 44.
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Article

A New Kv1.3 Channel Blocker from the Venom of the Ant Tetramorium bicarinatum

by
Guillaume Boy
1,
Laurence Jouvensal
2,3,
Nathan Téné
1,
Jean-Luc Carayon
1,
Elsa Bonnafé
1,
Françoise Paquet
2,
Michel Treilhou
1,
Karine Loth
2,3 and
Arnaud Billet
1,*
1
Equipe BTSB EA-7417, Institut National Universitaire Champollion, Place de Verdun, 81012 Albi, France
2
Centre de Biophysique Moléculaire, Centre National de la Recherche Scientifique (CNRS), Unité Propre de Recherche (UPR) 4301, 45071 Orléans, France
3
Unité de Formation et de Recherche (UFR) Sciences et Techniques, Université d’Orléans, 45071 Orléans, France
*
Author to whom correspondence should be addressed.
Toxins 2025, 17(8), 379; https://doi.org/10.3390/toxins17080379
Submission received: 13 June 2025 / Revised: 22 July 2025 / Accepted: 23 July 2025 / Published: 30 July 2025
(This article belongs to the Special Issue Unlocking the Deep Secrets of Toxins)
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Abstract

Ant venoms are rich sources of bioactive molecules, including peptide toxins with potent and selective activity on ion channels, which makes them valuable for pharmacological research and therapeutic development. Voltage-dependent potassium (Kv) channels, critical for regulating cellular excitability or cell cycle progression control, are targeted by a diverse array of venom-derived peptides. This study focuses on MYRTXA4-Tb11a, a peptide from Tetramorium bicarinatum venom, which was previously shown to have a strong paralytic effect on dipteran species without cytotoxicity on insect cells. In the present study, we show that Tb11a exhibited no or low cytotoxicity toward mammalian cells either, even at high concentrations, while electrophysiological studies revealed a blockade of hKv1.3 activity. Additionally, Ta11a, an analog of Tb11a from the ant Tetramorium africanum, demonstrated similar Kv1.3 inhibitory properties. Structural analysis supports that the peptide acts on Kv1.3 channels through the functional dyad Y21-K25 and that the disulfide bridge is essential for biological activity, as reduction seems to disrupt the peptide conformation and impair the dyad. These findings highlight the importance of three-dimensional structure in channel modulation and establish Tb11a and Ta11a as promising Kv1.3 inhibitors. Future research should investigate their selectivity across additional ion channels and employ structure-function studies to further enhance their pharmacological potential.
Keywords: ant venom peptide; Kv channels; functional dyad ant venom peptide; Kv channels; functional dyad

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MDPI and ACS Style

Boy, G.; Jouvensal, L.; Téné, N.; Carayon, J.-L.; Bonnafé, E.; Paquet, F.; Treilhou, M.; Loth, K.; Billet, A. A New Kv1.3 Channel Blocker from the Venom of the Ant Tetramorium bicarinatum. Toxins 2025, 17, 379. https://doi.org/10.3390/toxins17080379

AMA Style

Boy G, Jouvensal L, Téné N, Carayon J-L, Bonnafé E, Paquet F, Treilhou M, Loth K, Billet A. A New Kv1.3 Channel Blocker from the Venom of the Ant Tetramorium bicarinatum. Toxins. 2025; 17(8):379. https://doi.org/10.3390/toxins17080379

Chicago/Turabian Style

Boy, Guillaume, Laurence Jouvensal, Nathan Téné, Jean-Luc Carayon, Elsa Bonnafé, Françoise Paquet, Michel Treilhou, Karine Loth, and Arnaud Billet. 2025. "A New Kv1.3 Channel Blocker from the Venom of the Ant Tetramorium bicarinatum" Toxins 17, no. 8: 379. https://doi.org/10.3390/toxins17080379

APA Style

Boy, G., Jouvensal, L., Téné, N., Carayon, J.-L., Bonnafé, E., Paquet, F., Treilhou, M., Loth, K., & Billet, A. (2025). A New Kv1.3 Channel Blocker from the Venom of the Ant Tetramorium bicarinatum. Toxins, 17(8), 379. https://doi.org/10.3390/toxins17080379

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