Comparisons of Protein and Peptide Complexity in Poneroid and Formicoid Ant Venoms

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

Comparisons of Protein and Peptide Complexity in Poneroid and Formicoid Ant Venoms

Aili, SR Touchard, A Koh, JMS Dejean, A Orivel, J Padula, MP

Escoubas, P Nicholson, GM

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Publication Type:: Journal Article
Citation:: Journal of Proteome Research, 2016, 15 (9), pp. 3039 - 3054
Issue Date:: 2016-09-02

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Field	Value	Language
dc.contributor.author	Aili, SR	en_US
dc.contributor.author	Touchard, A	en_US
dc.contributor.author	Koh, JMS	en_US
dc.contributor.author	Dejean, A	en_US
dc.contributor.author	Orivel, J	en_US
dc.contributor.author	Padula, MP https://orcid.org/0000-0002-8283-0643	en_US
dc.contributor.author	Escoubas, P	en_US
dc.contributor.author	Nicholson, GM https://orcid.org/0000-0002-4277-4296	en_US
dc.date.available	2020-05-25T19:05:24Z
dc.date.issued	2016-09-02	en_US
dc.identifier.citation	Journal of Proteome Research, 2016, 15 (9), pp. 3039 - 3054	en_US
dc.identifier.issn	1535-3893	en_US
dc.identifier.uri	http://hdl.handle.net/10453/50383
dc.description.abstract	© 2016 American Chemical Society. 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.	en_US
dc.relation.ispartof	Journal of Proteome Research	en_US
dc.relation.isbasedon	10.1021/acs.jproteome.6b00182	en_US
dc.subject.classification	Biochemistry & Molecular Biology	en_US
dc.subject.mesh	Animals	en_US
dc.subject.mesh	Ants	en_US
dc.subject.mesh	Peptides	en_US
dc.subject.mesh	Proteins	en_US
dc.subject.mesh	Ant Venoms	en_US
dc.subject.mesh	Chromatography, High Pressure Liquid	en_US
dc.subject.mesh	Electrophoresis, Gel, Two-Dimensional	en_US
dc.subject.mesh	Species Specificity	en_US
dc.subject.mesh	Genetic Heterogeneity	en_US
dc.subject.mesh	Molecular Weight	en_US
dc.subject.mesh	Tandem Mass Spectrometry	en_US
dc.title	Comparisons of Protein and Peptide Complexity in Poneroid and Formicoid Ant Venoms	en_US
dc.type	Journal Article
utslib.citation.volume	9	en_US
utslib.citation.volume	15	en_US
utslib.for	1115 Pharmacology and Pharmaceutical Sciences	en_US
utslib.for	0601 Biochemistry and Cell Biology	en_US
utslib.for	03 Chemical 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/Faculty of Science/School of Life Sciences
pubs.organisational-group	/University of Technology Sydney/Strength - CHT - Health Technologies
utslib.copyright.status	open_access
pubs.issue	9	en_US
pubs.publication-status	Published	en_US
pubs.volume	15	en_US

Abstract:

© 2016 American Chemical Society. 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.

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http://hdl.handle.net/10453/50383