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

Identifieur interne : 002583 ( PubMed/Checkpoint ); précédent : 002582; suivant : 002584

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

Auteurs : Axel Touchard [France] ; Jennifer M S. Koh [Australie] ; Samira R. Aili [Australie] ; Alain Dejean [France] ; Graham M. Nicholson [Australie] ; Jérôme Orivel [France] ; Pierre Escoubas [France]

Source :

RBID : pubmed:26349460

Descripteurs français

English descriptors

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.

DOI: 10.1002/rcm.7116
PubMed: 26349460


Affiliations:


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pubmed:26349460

Le document en format XML

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<div type="abstract" xml:lang="en">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.</div>
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<AbstractText Label="METHODS" NlmCategory="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.</AbstractText>
<AbstractText Label="RESULTS" NlmCategory="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.</AbstractText>
<AbstractText Label="CONCLUSIONS" NlmCategory="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.</AbstractText>
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