Evidence map›Paper›PMID 42283821›Full record

ArticleCellular and molecular life sciences : CMLS2026

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

Suwatjanee Naephrai, Hue N T Tran, Thomas Durek, Axel Touchard, Vanessa Schendel, William Atherton, Irina Vetter, Panchika Prangkio, Samuel D Robinson

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Article in Cellular and molecular life sciences : CMLS, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

9 authors.

Suwatjanee NaephraiDepartment of Chemistry, Faculty of Science, Chiang Mai University, Chiang Mai, 50200, Thailand.
Hue N T TranInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, 4072, Australia.
Thomas DurekInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, 4072, Australia.
Axel TouchardCNRS, UMR Ecologie des forêts de Guyane - EcoFoG, Campus Agronomique, BP 316, Kourou Cedex, 97379, France.
Vanessa SchendelInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, 4072, Australia.
William AthertonInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, 4072, Australia.
Irina VetterInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, 4072, Australia.
Panchika PrangkioDepartment of Chemistry, Faculty of Science, Chiang Mai University, Chiang Mai, 50200, Thailand.
Samuel D RobinsonInstitute for Molecular Bioscience, The University of Queensland, Brisbane, QLD, 4072, Australia. sam.robinson@uq.edu.au.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

AntsAnt VenomsEvolution, MolecularPeptidesAmino Acid SequenceAnimalsMolecular Sequence DataPhylogenyProtein MultimerizationAnt VenomsPeptidesConvergent evolutionFormicidaeHeterodimerHomodimerPainPseudomyrmecinaeSting

Identifiers

PMID42283821
PMCPMC13486460

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