Venom composition of the ant Tetraponera rufonigra reveals insights into the evolution of dimeric ant venom peptides

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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Publication Details

Journal
Cellular and Molecular Life Sciences
Published
2026-06-12
DOI
https://doi.org/10.1007/s00018-026-06293-z
Primary Topic
Neurobiology and Insect Physiology Research
Type
article
Field-Weighted Citation Impact
0.00

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article

Venom composition of the ant Tetraponera rufonigra reveals insights into the evolution of dimeric ant venom peptides

Irina Vetter, Panchika Prangkio, Hue N. T. Tran, Vanessa Schendel et al.
Cellular and Molecular Life Sciences
Neurobiology and Insect Physiology Research
article

Venom composition of the ant Tetraponera rufonigra reveals insights into the evolution of dimeric ant venom peptides

Irina Vetter, Panchika Prangkio, Hue N. T. Tran, Vanessa Schendel, Suwatjanee Naephrai, Thomas Durek, Axel Touchard, S. Robinson, William Atherton
article en

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.

Cellular and Molecular Life Sciences
Centre National de la Recherche Scientifique (FR), Australian Research Council (AU), The University of Queensland (AU), North Chiang Mai University (TH), ARC Centre of Excellence for Innovations in Peptide and Protein Science (AU), Ecologie des Forêts de Guyane (GF), Chiang Mai University (TH)
University of Queensland
Openalex Percentile: Top 9%
Neurobiology and Insect Physiology Research
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Venom composition of the ant Tetraponera rufonigra reveals insights into the evolution of dimeric ant venom peptides — Irina Vetter, Panchika Prangkio, et al. · Cellular and Molecular Life Sciences (2026) | TGRS Research Map | TGRS