The complexity and structural diversity of ant venom peptidomes is revealed by mass spectrometry profiling

Rapid Communications in Mass Spectrometry : RCM
Axel TouchardP Escoubas

Abstract

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. 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. 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. The biochemical c...Continue Reading

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Citations

Jan 26, 2016·Toxins·Axel TouchardAlain Dejean
May 2, 2018·Toxicon : Official Journal of the International Society on Toxinology·José Roberto Aparecido Dos Santos-PintoMario Sergio Palma
Dec 22, 2020·ACS Pharmacology & Translational Science·Axel TouchardChristophe Duplais
Jul 21, 2016·Journal of Proteome Research·Samira R AiliGraham M Nicholson
Aug 29, 2018·Journal of Proteome Research·Axel TouchardElsa Bonnafé

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