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

Touchard, A; Koh, JMS; Aili, SR; Dejean, A; Nicholson, GM; Orivel, J; Escoubas, P

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

Touchard, A Koh, JMS Aili, SR Dejean, A Nicholson, GM

Orivel, J Escoubas, P

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Publication Type:: Journal Article
Citation:: Rapid Communications in Mass Spectrometry, 2015, 29 (5), pp. 385 - 396
Issue Date:: 2015-03-15

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Field	Value	Language
dc.contributor.author	Touchard, A	en_US
dc.contributor.author	Koh, JMS	en_US
dc.contributor.author	Aili, SR	en_US
dc.contributor.author	Dejean, A	en_US
dc.contributor.author	Nicholson, GM https://orcid.org/0000-0002-4277-4296	en_US
dc.contributor.author	Orivel, J	en_US
dc.contributor.author	Escoubas, P	en_US
dc.date.available	2014-12-03	en_US
dc.date.issued	2015-03-15	en_US
dc.identifier.citation	Rapid Communications in Mass Spectrometry, 2015, 29 (5), pp. 385 - 396	en_US
dc.identifier.issn	0951-4198	en_US
dc.identifier.uri	http://hdl.handle.net/10453/123698
dc.description.abstract	Copyright © 2015 John Wiley & Sons, Ltd. Rationale 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.	en_US
dc.relation.ispartof	Rapid Communications in Mass Spectrometry	en_US
dc.relation.isbasedon	10.1002/rcm.7116	en_US
dc.subject.classification	Analytical Chemistry	en_US
dc.subject.mesh	Animals	en_US
dc.subject.mesh	Ants	en_US
dc.subject.mesh	Disulfides	en_US
dc.subject.mesh	Peptides	en_US
dc.subject.mesh	Proteome	en_US
dc.subject.mesh	Ant Venoms	en_US
dc.subject.mesh	Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization	en_US
dc.title	The complexity and structural diversity of ant venom peptidomes is revealed by mass spectrometry profiling	en_US
dc.type	Journal Article
utslib.citation.volume	5	en_US
utslib.citation.volume	29	en_US
utslib.for	0301 Analytical Chemistry	en_US
utslib.for	0601 Biochemistry and Cell Biology	en_US
utslib.for	03 Chemical Sciences	en_US
utslib.for	04 Earth Sciences	en_US
utslib.for	06 Biological Sciences	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - CHT - Health Technologies
utslib.copyright.status	closed_access
pubs.issue	5	en_US
pubs.publication-status	Published	en_US
pubs.volume	29	en_US

Abstract:

Copyright © 2015 John Wiley & Sons, Ltd. Rationale 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.

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http://hdl.handle.net/10453/123698