title: Diversity of peptide toxins from stinging ant venoms.
abstract: Ants (Hymenoptera: Formicidae) represent a taxonomically diverse group of arthropods comprising nearly 13,000 extant species. Sixteen ant subfamilies have individuals that possess a stinger and use their venom for purposes such as a defence against predators, competitors and microbial pathogens, for predation, as well as for social communication. They exhibit a range of activities including antimicrobial, haemolytic, cytolytic, paralytic, insecticidal and pain-producing pharmacologies. While ant venoms are known to be rich in alkaloids and hydrocarbons, ant venoms rich in peptides are becoming more common, yet remain understudied. Recent advances in mass spectrometry techniques have begun to reveal the true complexity of ant venom peptide composition. In the few venoms explored thus far, most peptide toxins appear to occur as small polycationic linear toxins, with antibacterial properties and insecticidal activity. Unlike other venomous animals, a number of ant venoms also contain a range of homodimeric and heterodimeric peptides with one or two interchain disulfide bonds possessing pore-forming, allergenic and paralytic actions. However, ant venoms seem to have only a small number of monomeric disulfide-linked peptides. The present review details the structure and pharmacology of known ant venom peptide toxins and their potential as a source of novel bioinsecticides and therapeutic agents.
authors.affiliation: Neurotoxin Research Group, School of Medical & Molecular Biosciences, University of Technology Sydney, NSW 2007, Australia.
authors.forename: Samira R
authors.initials: SR
authors.lastname: Aili
authors.affiliation: CNRS, UMR Écologie des Forêts de Guyane (EcoFoG), Campus Agronomique, BP 316, 97379 Kourou Cedex, France.
authors.forename: Axel
authors.initials: A
authors.lastname: Touchard
authors.affiliation: VenomeTech, 473 Route des Dolines - Villa 3, 06560 Valbonne, France.
authors.forename: Pierre
authors.initials: P
authors.lastname: Escoubas
authors.affiliation: Neurotoxin Research Group, School of Medical & Molecular Biosciences, University of Technology Sydney, NSW 2007, Australia.
authors.forename: Matthew P
authors.initials: MP
authors.lastname: Padula
authors.affiliation: CNRS, UMR Écologie des Forêts de Guyane (EcoFoG), Campus Agronomique, BP 316, 97379 Kourou Cedex, France.
authors.forename: Jérôme
authors.initials: J
authors.lastname: Orivel
authors.affiliation: CNRS, UMR Écologie des Forêts de Guyane (EcoFoG), Campus Agronomique, BP 316, 97379 Kourou Cedex, France; Laboratoire Écologie Fonctionnelle et Environnement, Université de Toulouse, 118 Route de Narbonne, 31062 Toulouse, France. Electronic address: alain.dejean@wanadoo.fr.
authors.forename: Alain
authors.initials: A
authors.lastname: Dejean
authors.affiliation: Neurotoxin Research Group, School of Medical & Molecular Biosciences, University of Technology Sydney, NSW 2007, Australia. Electronic address: Graham.Nicholson@uts.edu.au.
authors.forename: Graham M
authors.initials: GM
authors.lastname: Nicholson
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000862:Ant Venoms / Q000032:analysis* / Q000145:classification; D001000:Ants / Q000737:chemistry* / Q000235:genetics; D001483:Base Sequence; D044822:Biodiversity; D005075:Biological Evolution; D019281:Dimerization; D055808:Drug Discovery / Q000379:methods; D013058:Mass Spectrometry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000235:genetics* / Q000633:toxicity*; D010802:Phylogeny; D017422:Sequence Analysis, DNA; D013045:Species Specificity
chemical_list: D000862:Ant Venoms; D010455:Peptides
keywords: Ant venom; Chemotaxonomy; Disulfide linkage; Peptides; Venom biochemistry