Venom composition of the ant Tetraponera rufonigra reveals insights into the evolution of dimeric ant venom peptides
Abstract
The majority of ant species are venomous, and in most lineages, peptide toxins dominate venom composition. Here we investigated the venom of the ant Tetraponera rufonigra (subfamily Pseudomyrmecinae). The major active component, Tr1a, is a homodimeric peptide that is cytolytic, activates mammalian sensory neurons and is insecticidal. Structural analyses show that Tr1a consists of two identical peptide chains arranged as antiparallel α-helices and covalently linked by three interchain disulfide bonds, forming a symmetrical amphipathic dimer. We demonstrate that dimeric venom peptides with similar biological activities have evolved independently multiple times across ants. The repeated evolution of dimeric venom peptides in ants highlights the evolutionary plasticity of ant venom and the role of convergence in shaping ant venom composition.
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BibTeX
@article{naephrai2026venom,
title = {{Venom composition of the ant Tetraponera rufonigra reveals insights into the evolution of dimeric ant venom peptides}},
author = {Suwatjanee Naephrai and Hue N T Tran and Thomas Durek and Axel Touchard and Vanessa Schendel and William Atherton and Irina Vetter and Panchika Prangkio and Samuel D Robinson},
journal = {Cellular and Molecular Life Sciences},
year = {2026},
month = jun,
doi = {10.1007/s00018-026-06293-z},
url = {https://hal.science/hal-05737431v1},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Venom composition of the ant Tetraponera rufonigra reveals insights into the evolution of dimeric ant venom peptides
AU - Suwatjanee Naephrai
AU - Hue N T Tran
AU - Thomas Durek
AU - Axel Touchard
AU - Vanessa Schendel
AU - William Atherton
AU - Irina Vetter
AU - Panchika Prangkio
AU - Samuel D Robinson
PY - 2026
DA - 2026/06/12
JO - Cellular and Molecular Life Sciences
DO - 10.1007/s00018-026-06293-z
UR - https://hal.science/hal-05737431v1
AB - The majority of ant species are venomous, and in most lineages, peptide toxins dominate venom composition. Here we investigated the venom of the ant Tetraponera rufonigra (subfamily Pseudomyrmecinae). The major active component, Tr1a, is a homodimeric peptide that is cytolytic, activates mammalian sensory neurons and is insecticidal. Structural analyses show that Tr1a consists of two identical peptide chains arranged as antiparallel α-helices and covalently linked by three interchain disulfide bonds, forming a symmetrical amphipathic dimer. We demonstrate that dimeric venom peptides with similar biological activities have evolved independently multiple times across ants. The repeated evolution of dimeric venom peptides in ants highlights the evolutionary plasticity of ant venom and the role of convergence in shaping ant venom composition.
SN - 1420-682X
SN - 1420-9071
ER -