Abstract
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.
Highlights
Venoms are biochemical arsenals developed by animals to defend themselves and/or capture prey [1]
The initial liquid chromatography-mass spectrometry (LC–MS) analysis was performed on an LCQ-ion trap Advantage mass spectrometer in order to establish the list of the masses of the most abundant peptides in Tetraponera aethiops venom (Table 1)
The total ion chromatogram (TIC) analysis of the venom of T. aethiops revealed several peaks with 12 masses corresponding to peptides (Figure 1)
Summary
Venoms are biochemical arsenals developed by animals to defend themselves and/or capture prey [1]. Studies on arthropod (e.g., scorpions, spiders, centipedes, and insects) venoms show a majority of proteins and peptides which exhibit variable amino acid sequences and tridimensional structures in their mature form [2,3]. Most of these studies have focused on emblematic and/or problematic species whose stings are painful and can cause allergies [4,5,6], with the major goal being to relieve the symptoms prompted by these venoms. The painful venoms of the bullet ant Paraponera clavata and of ponerine ants of the genera Dinoponera and Neoponera have been the subject of several studies which led to the isolation and characterization of tens of bioactive peptides [10,11]
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