title: Comparisons of Protein and Peptide Complexity in Poneroid and Formicoid Ant Venoms.
abstract: Animal venom peptides are currently being developed as novel drugs and bioinsecticides. Because ants use venoms for defense and predation, venomous ants represent an untapped source of potential bioactive toxins. This study compared the protein and peptide components of the poneroid ants Neoponera commutata, Neoponera apicalis, and Odontomachus hastatus and the formicoid ants Ectatomma tuberculatum, Ectatomma brunneum, and Myrmecia gulosa. 1D and 2D PAGE revealed venom proteins in the mass range <10 to >250 kDa. NanoLC-ESI-QTOF MS/MS analysis of tryptic peptides revealed the presence of common venom proteins and also many undescribed proteins. RP-HPLC separation followed by MALDI-TOF MS of the venom peptides also revealed considerable heterogeneity. It was found that the venoms contained between 144 and 1032 peptides with 5-95% of peptides in the ranges 1-4 and 1-8 kDa for poneroid and formicoid ants, respectively. By employing the reducing MALDI matrix 1,5-diaminonapthalene, up to 28 disulfide-bonded peptides were also identified in each of the venoms. In particular, the mass range of peptides from poneroid ants is lower than peptides from other venoms, indicating possible novel structures and pharmacologies. These results indicate that ant venoms represent an enormous, untapped source of novel therapeutic and bioinsecticide leads.
authors.affiliation: Neurotoxin Research Group, School of Life Sciences, Faculty of Science, University of Technology Sydney , Sydney, New South Wales 2007, Australia.
authors.forename: Samira R
authors.initials: SR
authors.lastname: Aili
authors.affiliation: CNRS , UMR Ecologie des Forêts de Guyane (EcoFoG), Campus Agronomique, BP 316, 97379 Kourou Cedex, France.
authors.forename: Axel
authors.initials: A
authors.lastname: Touchard
authors.affiliation: Neurotoxin Research Group, School of Life Sciences, Faculty of Science, University of Technology Sydney , Sydney, New South Wales 2007, Australia.
authors.forename: Jennifer M S
authors.initials: JM
authors.lastname: Koh
authors.affiliation: CNRS , UMR Ecologie des Forêts de Guyane (EcoFoG), Campus Agronomique, BP 316, 97379 Kourou Cedex, France.|Laboratoire Écologie Fonctionnelle et Environnement, CNRS, UMR 5245, Ecolab, 118 route de Narbonne, 31062 Toulouse, France.
authors.forename: Alain
authors.initials: A
authors.lastname: Dejean
authors.affiliation: CNRS , UMR Ecologie des Forêts de Guyane (EcoFoG), Campus Agronomique, BP 316, 97379 Kourou Cedex, France.
authors.forename: Jérôme
authors.initials: J
authors.lastname: Orivel
authors.affiliation: Proteomics Core Facility, Faculty of Science, University of Technology Sydney , Sydney, New South Wales 2007, Australia.
authors.forename: Matthew P
authors.initials: MP
authors.lastname: Padula
authors.affiliation: VenomeTech , 473 Route des Dolines - Villa 3, Valbonne 06560, France.
authors.forename: Pierre
authors.initials: P
authors.lastname: Escoubas
authors.affiliation: Neurotoxin Research Group, School of Life Sciences, Faculty of Science, University of Technology Sydney , Sydney, New South Wales 2007, Australia.
authors.forename: Graham M
authors.initials: GM
authors.lastname: Nicholson
mesh_terms: D000818:Animals; D000862:Ant Venoms / Q000737:chemistry*; D001000:Ants; D002851:Chromatography, High Pressure Liquid; D015180:Electrophoresis, Gel, Two-Dimensional; D018740:Genetic Heterogeneity; D008970:Molecular Weight; D010455:Peptides / Q000032:analysis*; D011506:Proteins / Q000032:analysis*; D013045:Species Specificity; D053719:Tandem Mass Spectrometry
chemical_list: D000862:Ant Venoms; D010455:Peptides; D011506:Proteins
keywords: Hymenoptera; LC-MALDI-TOF MS; ant venom; mass spectrometry; nanoLC-ESI-QTOF MS/MS; peptidome; proteomic analysis; toxin