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The Peptide Venom Composition of the Fierce Stinging Ant Tetraponera aethiops (Formicidae: Pseudomyrmecinae)

In the mutualisms involving certain pseudomyrmicine ants and different myrmecophytes (i.e., plants sheltering colonies of specialized “plant-ant” species in hollow structures), the ant venom contributes to the host plant biotic defenses by inducing the rapid paralysis of defoliating insects and caus...

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Autores principales: Barassé, Valentine, Touchard, Axel, Téné, Nathan, Tindo, Maurice, Kenne, Martin, Klopp, Christophe, Dejean, Alain, Bonnafé, Elsa, Treilhou, Michel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6950161/
https://www.ncbi.nlm.nih.gov/pubmed/31847368
http://dx.doi.org/10.3390/toxins11120732
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author Barassé, Valentine
Touchard, Axel
Téné, Nathan
Tindo, Maurice
Kenne, Martin
Klopp, Christophe
Dejean, Alain
Bonnafé, Elsa
Treilhou, Michel
author_facet Barassé, Valentine
Touchard, Axel
Téné, Nathan
Tindo, Maurice
Kenne, Martin
Klopp, Christophe
Dejean, Alain
Bonnafé, Elsa
Treilhou, Michel
author_sort Barassé, Valentine
collection PubMed
description In the mutualisms involving certain pseudomyrmicine ants and different myrmecophytes (i.e., plants sheltering colonies of specialized “plant-ant” species in hollow structures), the ant venom contributes to the host plant biotic defenses by inducing the rapid paralysis of defoliating insects and causing intense pain to browsing mammals. Using integrated transcriptomic and proteomic approaches, we identified the venom peptidome of the plant-ant Tetraponera aethiops (Pseudomyrmecinae). The transcriptomic analysis of its venom glands revealed that 40% of the expressed contigs encoded only seven peptide precursors related to the ant venom peptides from the A-superfamily. Among the 12 peptide masses detected by liquid chromatography-mass spectrometry (LC–MS), nine mature peptide sequences were characterized and confirmed through proteomic analysis. These venom peptides, called pseudomyrmecitoxins (PSDTX), share amino acid sequence identities with myrmeciitoxins known for their dual offensive and defensive functions on both insects and mammals. Furthermore, we demonstrated through reduction/alkylation of the crude venom that four PSDTXs were homo- and heterodimeric. Thus, we provide the first insights into the defensive venom composition of the ant genus Tetraponera indicative of a streamlined peptidome.
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spelling pubmed-69501612020-01-13 The Peptide Venom Composition of the Fierce Stinging Ant Tetraponera aethiops (Formicidae: Pseudomyrmecinae) Barassé, Valentine Touchard, Axel Téné, Nathan Tindo, Maurice Kenne, Martin Klopp, Christophe Dejean, Alain Bonnafé, Elsa Treilhou, Michel Toxins (Basel) Article In the mutualisms involving certain pseudomyrmicine ants and different myrmecophytes (i.e., plants sheltering colonies of specialized “plant-ant” species in hollow structures), the ant venom contributes to the host plant biotic defenses by inducing the rapid paralysis of defoliating insects and causing intense pain to browsing mammals. Using integrated transcriptomic and proteomic approaches, we identified the venom peptidome of the plant-ant Tetraponera aethiops (Pseudomyrmecinae). The transcriptomic analysis of its venom glands revealed that 40% of the expressed contigs encoded only seven peptide precursors related to the ant venom peptides from the A-superfamily. Among the 12 peptide masses detected by liquid chromatography-mass spectrometry (LC–MS), nine mature peptide sequences were characterized and confirmed through proteomic analysis. These venom peptides, called pseudomyrmecitoxins (PSDTX), share amino acid sequence identities with myrmeciitoxins known for their dual offensive and defensive functions on both insects and mammals. Furthermore, we demonstrated through reduction/alkylation of the crude venom that four PSDTXs were homo- and heterodimeric. Thus, we provide the first insights into the defensive venom composition of the ant genus Tetraponera indicative of a streamlined peptidome. MDPI 2019-12-14 /pmc/articles/PMC6950161/ /pubmed/31847368 http://dx.doi.org/10.3390/toxins11120732 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Barassé, Valentine
Touchard, Axel
Téné, Nathan
Tindo, Maurice
Kenne, Martin
Klopp, Christophe
Dejean, Alain
Bonnafé, Elsa
Treilhou, Michel
The Peptide Venom Composition of the Fierce Stinging Ant Tetraponera aethiops (Formicidae: Pseudomyrmecinae)
title The Peptide Venom Composition of the Fierce Stinging Ant Tetraponera aethiops (Formicidae: Pseudomyrmecinae)
title_full The Peptide Venom Composition of the Fierce Stinging Ant Tetraponera aethiops (Formicidae: Pseudomyrmecinae)
title_fullStr The Peptide Venom Composition of the Fierce Stinging Ant Tetraponera aethiops (Formicidae: Pseudomyrmecinae)
title_full_unstemmed The Peptide Venom Composition of the Fierce Stinging Ant Tetraponera aethiops (Formicidae: Pseudomyrmecinae)
title_short The Peptide Venom Composition of the Fierce Stinging Ant Tetraponera aethiops (Formicidae: Pseudomyrmecinae)
title_sort peptide venom composition of the fierce stinging ant tetraponera aethiops (formicidae: pseudomyrmecinae)
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6950161/
https://www.ncbi.nlm.nih.gov/pubmed/31847368
http://dx.doi.org/10.3390/toxins11120732
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