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Journal Article

Citation

Touchard A, Labrière N, Roux O, Petitclerc F, Orivel J, Escoubas P, Koh JM, Nicholson GM, Dejean A. Toxicon 2014; 88: 67-76.

Affiliation

CNRS, UMR Ecologie des Forêts de Guyane (EcoFoG), Campus Agronomique, BP 316, 97379 Kourou Cedex, France; Laboratoire Écologie Fonctionnelle et Environnement, 118 route de Narbonne, 31062 Toulouse, France. Electronic address: alain.dejean@wanadoo.fr.

Copyright

(Copyright © 2014, Elsevier Publishing)

DOI

10.1016/j.toxicon.2014.05.022

PMID

24929139

Abstract

We aimed to determine whether the nesting habits of ants have influenced their venom toxicity and composition. We focused on the genus Pseudomyrmex (Pseudomyrmecinae) comprising terrestrial and arboreal species, and, among the latter, plant-ants that are obligate inhabitants of myrmecophytes (i.e., plants sheltering ants in hollow structures). Contrary to our hypothesis, the venom of the ground-dwelling species, P. termitarius, was as efficacious in paralyzing prey as the venoms of the arboreal and the plant-ant species, P. penetrator and P. gracilis. The lethal potency of P. termitarius venom was equipotent with that of P. gracilis whereas the venom of P. penetrator was less potent. The MALDI-TOF MS analysis of each HPLC fraction of the venoms showed that P. termitarius venom is composed of 87 linear peptides, while both P. gracilis and P. penetrator venoms (23 and 26 peptides, respectively) possess peptides with disulfide bonds. Furthermore, P. penetrator venom contains three hetero- and homodimeric peptides consisting of two short peptidic chains linked together by two interchain disulfide bonds. The large number of peptides in P. termitarius venom is likely related to the large diversity of potential prey plus the antibacterial peptides required for nesting in the ground. Whereas predation involves only the prey and predator, P. penetrator venom has evolved in an environment where trees, defoliating insects, browsing mammals and ants live in equilibrium, likely explaining the diversity of the peptide structures.


Language: en

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