Comparisons of Protein and Peptide Complexity in Poneroid and Formicoid Ant Venoms.
Identifieur interne : 002190 ( Main/Exploration ); précédent : 002189; suivant : 002191Comparisons of Protein and Peptide Complexity in Poneroid and Formicoid Ant Venoms.
Auteurs : Samira R. Aili [Australie] ; Axel Touchard [France] ; Jennifer M S. Koh [Australie] ; Alain Dejean [France] ; Jérôme Orivel [France] ; Matthew P. Padula [Australie] ; Pierre Escoubas [France] ; Graham M. Nicholson [Australie]Source :
- Journal of proteome research [ 1535-3907 ] ; 2016.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , analysis : Peptides, Proteins.
- chemical , chemistry : Ant Venoms.
- Animals, Ants, Chromatography, High Pressure Liquid, Electrophoresis, Gel, Two-Dimensional, Genetic Heterogeneity, Molecular Weight, Species Specificity, Tandem Mass Spectrometry.
Abstract
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.
DOI: 10.1021/acs.jproteome.6b00182
PubMed: 27436154
Affiliations:
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Aili</name><affiliation wicri:level="1"><nlm:affiliation>Neurotoxin Research Group, School of Life Sciences, Faculty of Science, University of Technology Sydney , Sydney, New South Wales 2007, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Neurotoxin Research Group, School of Life Sciences, Faculty of Science, University of Technology Sydney , Sydney, New South Wales 2007</wicri:regionArea><wicri:noRegion>New South Wales 2007</wicri:noRegion></affiliation></author><author><name sortKey="Touchard, Axel" sort="Touchard, Axel" uniqKey="Touchard A" first="Axel" last="Touchard">Axel Touchard</name><affiliation wicri:level="1"><nlm:affiliation>CNRS , UMR Ecologie des Forêts de Guyane (EcoFoG), Campus Agronomique, BP 316, 97379 Kourou Cedex, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>CNRS , UMR Ecologie des Forêts de Guyane (EcoFoG), Campus Agronomique, BP 316, 97379 Kourou Cedex</wicri:regionArea><wicri:noRegion>97379 Kourou Cedex</wicri:noRegion><wicri:noRegion>97379 Kourou Cedex</wicri:noRegion></affiliation></author><author><name sortKey="Koh, Jennifer M S" sort="Koh, Jennifer M S" uniqKey="Koh J" first="Jennifer M S" last="Koh">Jennifer M S. Koh</name><affiliation wicri:level="1"><nlm:affiliation>Neurotoxin Research Group, School of Life Sciences, Faculty of Science, University of Technology Sydney , Sydney, New South Wales 2007, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Neurotoxin Research Group, School of Life Sciences, Faculty of Science, University of Technology Sydney , Sydney, New South Wales 2007</wicri:regionArea><wicri:noRegion>New South Wales 2007</wicri:noRegion></affiliation></author><author><name sortKey="Dejean, Alain" sort="Dejean, Alain" uniqKey="Dejean A" first="Alain" last="Dejean">Alain Dejean</name><affiliation wicri:level="1"><nlm:affiliation>CNRS , UMR Ecologie des Forêts de Guyane (EcoFoG), Campus Agronomique, BP 316, 97379 Kourou Cedex, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>CNRS , UMR Ecologie des Forêts de Guyane (EcoFoG), Campus Agronomique, BP 316, 97379 Kourou Cedex</wicri:regionArea><wicri:noRegion>97379 Kourou Cedex</wicri:noRegion><wicri:noRegion>97379 Kourou Cedex</wicri:noRegion></affiliation></author><author><name sortKey="Orivel, Jerome" sort="Orivel, Jerome" uniqKey="Orivel J" first="Jérôme" last="Orivel">Jérôme Orivel</name><affiliation wicri:level="1"><nlm:affiliation>CNRS , UMR Ecologie des Forêts de Guyane (EcoFoG), Campus Agronomique, BP 316, 97379 Kourou Cedex, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>CNRS , UMR Ecologie des Forêts de Guyane (EcoFoG), Campus Agronomique, BP 316, 97379 Kourou Cedex</wicri:regionArea><wicri:noRegion>97379 Kourou Cedex</wicri:noRegion><wicri:noRegion>97379 Kourou Cedex</wicri:noRegion></affiliation></author><author><name sortKey="Padula, Matthew P" sort="Padula, Matthew P" uniqKey="Padula M" first="Matthew P" last="Padula">Matthew P. Padula</name><affiliation wicri:level="1"><nlm:affiliation>Proteomics Core Facility, Faculty of Science, University of Technology Sydney , Sydney, New South Wales 2007, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Proteomics Core Facility, Faculty of Science, University of Technology Sydney , Sydney, New South Wales 2007</wicri:regionArea><wicri:noRegion>New South Wales 2007</wicri:noRegion></affiliation></author><author><name sortKey="Escoubas, Pierre" sort="Escoubas, Pierre" uniqKey="Escoubas P" first="Pierre" last="Escoubas">Pierre Escoubas</name><affiliation wicri:level="1"><nlm:affiliation>VenomeTech , 473 Route des Dolines - Villa 3, Valbonne 06560, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>VenomeTech , 473 Route des Dolines - Villa 3, Valbonne 06560</wicri:regionArea><wicri:noRegion>06560</wicri:noRegion><wicri:noRegion>06560</wicri:noRegion></affiliation></author><author><name sortKey="Nicholson, Graham M" sort="Nicholson, Graham M" uniqKey="Nicholson G" first="Graham M" last="Nicholson">Graham M. Nicholson</name><affiliation wicri:level="1"><nlm:affiliation>Neurotoxin Research Group, School of Life Sciences, Faculty of Science, University of Technology Sydney , Sydney, New South Wales 2007, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Neurotoxin Research Group, School of Life Sciences, Faculty of Science, University of Technology Sydney , Sydney, New South Wales 2007</wicri:regionArea><wicri:noRegion>New South Wales 2007</wicri:noRegion></affiliation></author></analytic><series><title level="j">Journal of proteome research</title><idno type="eISSN">1535-3907</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Ant Venoms (chemistry)</term><term>Ants</term><term>Chromatography, High Pressure Liquid</term><term>Electrophoresis, Gel, Two-Dimensional</term><term>Genetic Heterogeneity</term><term>Molecular Weight</term><term>Peptides (analysis)</term><term>Proteins (analysis)</term><term>Species Specificity</term><term>Tandem Mass Spectrometry</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Chromatographie en phase liquide à haute performance</term><term>Fourmis</term><term>Hétérogénéité génétique</term><term>Masse moléculaire</term><term>Peptides (analyse)</term><term>Protéines (analyse)</term><term>Spectrométrie de masse en tandem</term><term>Spécificité d'espèce</term><term>Venins de fourmi ()</term><term>Électrophorèse bidimensionnelle sur gel</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Peptides</term><term>Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Ant Venoms</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Peptides</term><term>Protéines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Ants</term><term>Chromatography, High Pressure Liquid</term><term>Electrophoresis, Gel, Two-Dimensional</term><term>Genetic Heterogeneity</term><term>Molecular Weight</term><term>Species Specificity</term><term>Tandem Mass Spectrometry</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Chromatographie en phase liquide à haute performance</term><term>Fourmis</term><term>Hétérogénéité génétique</term><term>Masse moléculaire</term><term>Spectrométrie de masse en tandem</term><term>Spécificité d'espèce</term><term>Venins de fourmi</term><term>Électrophorèse bidimensionnelle sur gel</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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.</div></front></TEI><affiliations><list><country><li>Australie</li><li>France</li></country></list><tree><country name="Australie"><noRegion><name sortKey="Aili, Samira R" sort="Aili, Samira R" uniqKey="Aili S" first="Samira R" last="Aili">Samira R. Aili</name></noRegion><name sortKey="Koh, Jennifer M S" sort="Koh, Jennifer M S" uniqKey="Koh J" first="Jennifer M S" last="Koh">Jennifer M S. Koh</name><name sortKey="Nicholson, Graham M" sort="Nicholson, Graham M" uniqKey="Nicholson G" first="Graham M" last="Nicholson">Graham M. Nicholson</name><name sortKey="Padula, Matthew P" sort="Padula, Matthew P" uniqKey="Padula M" first="Matthew P" last="Padula">Matthew P. Padula</name></country><country name="France"><noRegion><name sortKey="Touchard, Axel" sort="Touchard, Axel" uniqKey="Touchard A" first="Axel" last="Touchard">Axel Touchard</name></noRegion><name sortKey="Dejean, Alain" sort="Dejean, Alain" uniqKey="Dejean A" first="Alain" last="Dejean">Alain Dejean</name><name sortKey="Escoubas, Pierre" sort="Escoubas, Pierre" uniqKey="Escoubas P" first="Pierre" last="Escoubas">Pierre Escoubas</name><name sortKey="Orivel, Jerome" sort="Orivel, Jerome" uniqKey="Orivel J" first="Jérôme" last="Orivel">Jérôme Orivel</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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