The complexity and structural diversity of ant venom peptidomes is revealed by mass spectrometry profiling.
BACKGROUND
Compared with other animal venoms, ant venoms remain little explored. Ants have evolved complex venoms to rapidly immobilize arthropod prey and to protect their colonies from predators and pathogens. Many ants have retained peptide-rich venoms that are similar to those of other arthropod groups.


METHODS
With the goal of conducting a broad and comprehensive survey of ant venom peptide diversity, we investigated the peptide composition of venoms from 82 stinging ant species from nine subfamilies using matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry (MALDI-TOFMS). We also conducted an in-depth investigation of eight venoms using reversed-phase high-performance liquid chromatography (RP-HPLC) separation coupled with offline MALDI-TOFMS.


RESULTS
Our results reveal that the peptide compositions of ant venom peptidomes from both poneroid and formicoid ant clades comprise hundreds of small peptides (<4 kDa), while large peptides (>4 kDa) are also present in the venom of formicoids. Chemical reduction revealed the presence of disulfide-linked peptides in most ant subfamilies, including peptides structured by one, two or three disulfide bonds as well as dimeric peptides reticulated by three disulfide bonds.


CONCLUSIONS
The biochemical complexity of ant venoms, associated with an enormous ecological and taxonomic diversity, suggests that stinging ant venoms constitute a promising source of bioactive molecules that could be exploited in the search for novel drug and biopesticide leads.
CNRS, UMR Ecologie des Forêts de Guyane (EcoFoG), Campus Agronomique, BP 316, 97379, Kourou Cedex, France.
Axel
A
Touchard
Neurotoxin Research Group, School of Medical & Molecular Biosciences, University of Technology, Sydney, NSW, Australia.
Jennifer M S
JM
Koh
Neurotoxin Research Group, School of Medical & Molecular Biosciences, University of Technology, Sydney, NSW, Australia.
Samira R
SR
Aili
CNRS, UMR Ecologie des Forêts de Guyane (EcoFoG), Campus Agronomique, BP 316, 97379, Kourou Cedex, France.|Laboratoire Écologie Fonctionnelle et Environnement, Université de Toulouse, Toulouse, France.
Alain
A
Dejean
Neurotoxin Research Group, School of Medical & Molecular Biosciences, University of Technology, Sydney, NSW, Australia.
Graham M
GM
Nicholson
CNRS, UMR Ecologie des Forêts de Guyane (EcoFoG), Campus Agronomique, BP 316, 97379, Kourou Cedex, France.
Jérôme
J
Orivel
VenomeTech, 473 Route des Dolines, Valbonne, 06560,, France.
Pierre
P
Escoubas
D000818:Animals; D000862:Ant Venoms / Q000032:analysis* / Q000737:chemistry; D001000:Ants; D004220:Disulfides; D010455:Peptides / Q000032:analysis* / Q000737:chemistry; D020543:Proteome / Q000032:analysis* / Q000737:chemistry; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*
D000862:Ant Venoms; D004220:Disulfides; D010455:Peptides; D020543:Proteome