Diversity of peptide toxins from stinging ant venoms.
Identifieur interne : 002040 ( Ncbi/Merge ); précédent : 002039; suivant : 002041Diversity of peptide toxins from stinging ant venoms.
Auteurs : Samira R. Aili [Australie] ; Axel Touchard [France] ; Pierre Escoubas [France] ; Matthew P. Padula [Australie] ; Jérôme Orivel [France] ; Alain Dejean [France] ; Graham M. Nicholson [Australie]Source :
- Toxicon : official journal of the International Society on Toxinology [ 1879-3150 ] ; 2014.
Descripteurs français
- KwdFr :
- Analyse de séquence d'ADN, Animaux, Biodiversité, Dimérisation, Données de séquences moléculaires, Découverte de médicament (), Fourmis (), Fourmis (génétique), Modèles moléculaires, Peptides (génétique), Peptides (toxicité), Phylogénie, Spectrométrie de masse, Spécificité d'espèce, Séquence d'acides aminés, Séquence nucléotidique, Venins de fourmi (), Venins de fourmi (analyse), Évolution biologique.
- MESH :
- analyse : Venins de fourmi.
- génétique : Fourmis, Peptides.
- toxicité : Peptides.
- Analyse de séquence d'ADN, Animaux, Biodiversité, Dimérisation, Données de séquences moléculaires, Découverte de médicament, Fourmis, Modèles moléculaires, Phylogénie, Spectrométrie de masse, Spécificité d'espèce, Séquence d'acides aminés, Séquence nucléotidique, Venins de fourmi, Évolution biologique.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Ant Venoms (analysis), Ant Venoms (classification), Ants (chemistry), Ants (genetics), Base Sequence, Biodiversity, Biological Evolution, Dimerization, Drug Discovery (methods), Mass Spectrometry, Models, Molecular, Molecular Sequence Data, Peptides (genetics), Peptides (toxicity), Phylogeny, Sequence Analysis, DNA, Species Specificity.
- MESH :
- chemical , analysis : Ant Venoms.
- chemical , classification : Ant Venoms.
- chemistry : Ants.
- genetics : Ants, Peptides.
- methods : Drug Discovery.
- chemical , toxicity : Peptides.
- Amino Acid Sequence, Animals, Base Sequence, Biodiversity, Biological Evolution, Dimerization, Mass Spectrometry, Models, Molecular, Molecular Sequence Data, Phylogeny, Sequence Analysis, DNA, Species Specificity.
Abstract
Ants (Hymenoptera: Formicidae) represent a taxonomically diverse group of arthropods comprising nearly 13,000 extant species. Sixteen ant subfamilies have individuals that possess a stinger and use their venom for purposes such as a defence against predators, competitors and microbial pathogens, for predation, as well as for social communication. They exhibit a range of activities including antimicrobial, haemolytic, cytolytic, paralytic, insecticidal and pain-producing pharmacologies. While ant venoms are known to be rich in alkaloids and hydrocarbons, ant venoms rich in peptides are becoming more common, yet remain understudied. Recent advances in mass spectrometry techniques have begun to reveal the true complexity of ant venom peptide composition. In the few venoms explored thus far, most peptide toxins appear to occur as small polycationic linear toxins, with antibacterial properties and insecticidal activity. Unlike other venomous animals, a number of ant venoms also contain a range of homodimeric and heterodimeric peptides with one or two interchain disulfide bonds possessing pore-forming, allergenic and paralytic actions. However, ant venoms seem to have only a small number of monomeric disulfide-linked peptides. The present review details the structure and pharmacology of known ant venom peptide toxins and their potential as a source of novel bioinsecticides and therapeutic agents.
DOI: 10.1016/j.toxicon.2014.10.021
PubMed: 25448389
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pubmed:25448389Le document en format XML
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Electronic address: Graham.Nicholson@uts.edu.au.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Neurotoxin Research Group, School of Medical & Molecular Biosciences, University of Technology Sydney, NSW 2007</wicri:regionArea><wicri:noRegion>NSW 2007</wicri:noRegion></affiliation></author></analytic><series><title level="j">Toxicon : official journal of the International Society on Toxinology</title><idno type="eISSN">1879-3150</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Ant Venoms (analysis)</term><term>Ant Venoms (classification)</term><term>Ants (chemistry)</term><term>Ants (genetics)</term><term>Base Sequence</term><term>Biodiversity</term><term>Biological Evolution</term><term>Dimerization</term><term>Drug Discovery (methods)</term><term>Mass Spectrometry</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Peptides (genetics)</term><term>Peptides (toxicity)</term><term>Phylogeny</term><term>Sequence Analysis, DNA</term><term>Species Specificity</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Analyse de séquence d'ADN</term><term>Animaux</term><term>Biodiversité</term><term>Dimérisation</term><term>Données de séquences moléculaires</term><term>Découverte de médicament ()</term><term>Fourmis ()</term><term>Fourmis (génétique)</term><term>Modèles moléculaires</term><term>Peptides (génétique)</term><term>Peptides (toxicité)</term><term>Phylogénie</term><term>Spectrométrie de masse</term><term>Spécificité d'espèce</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Venins de fourmi ()</term><term>Venins de fourmi (analyse)</term><term>Évolution biologique</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Ant Venoms</term></keywords><keywords scheme="MESH" type="chemical" qualifier="classification" xml:lang="en"><term>Ant Venoms</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Venins de fourmi</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Ants</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Ants</term><term>Peptides</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Fourmis</term><term>Peptides</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Drug Discovery</term></keywords><keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Peptides</term></keywords><keywords scheme="MESH" qualifier="toxicité" xml:lang="fr"><term>Peptides</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Biodiversity</term><term>Biological Evolution</term><term>Dimerization</term><term>Mass Spectrometry</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Phylogeny</term><term>Sequence Analysis, DNA</term><term>Species Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse de séquence d'ADN</term><term>Animaux</term><term>Biodiversité</term><term>Dimérisation</term><term>Données de séquences moléculaires</term><term>Découverte de médicament</term><term>Fourmis</term><term>Modèles moléculaires</term><term>Phylogénie</term><term>Spectrométrie de masse</term><term>Spécificité d'espèce</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Venins de fourmi</term><term>Évolution biologique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Ants (Hymenoptera: Formicidae) represent a taxonomically diverse group of arthropods comprising nearly 13,000 extant species. Sixteen ant subfamilies have individuals that possess a stinger and use their venom for purposes such as a defence against predators, competitors and microbial pathogens, for predation, as well as for social communication. They exhibit a range of activities including antimicrobial, haemolytic, cytolytic, paralytic, insecticidal and pain-producing pharmacologies. While ant venoms are known to be rich in alkaloids and hydrocarbons, ant venoms rich in peptides are becoming more common, yet remain understudied. Recent advances in mass spectrometry techniques have begun to reveal the true complexity of ant venom peptide composition. In the few venoms explored thus far, most peptide toxins appear to occur as small polycationic linear toxins, with antibacterial properties and insecticidal activity. Unlike other venomous animals, a number of ant venoms also contain a range of homodimeric and heterodimeric peptides with one or two interchain disulfide bonds possessing pore-forming, allergenic and paralytic actions. However, ant venoms seem to have only a small number of monomeric disulfide-linked peptides. The present review details the structure and pharmacology of known ant venom peptide toxins and their potential as a source of novel bioinsecticides and therapeutic agents.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25448389</PMID><DateCreated><Year>2014</Year><Month>12</Month><Day>18</Day></DateCreated><DateCompleted><Year>2015</Year><Month>07</Month><Day>27</Day></DateCompleted><DateRevised><Year>2014</Year><Month>12</Month><Day>18</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-3150</ISSN><JournalIssue CitedMedium="Internet"><Volume>92</Volume><PubDate><Year>2014</Year><Month>Dec</Month><Day>15</Day></PubDate></JournalIssue><Title>Toxicon : official journal of the International Society on Toxinology</Title><ISOAbbreviation>Toxicon</ISOAbbreviation></Journal><ArticleTitle>Diversity of peptide toxins from stinging ant venoms.</ArticleTitle><Pagination><MedlinePgn>166-78</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.toxicon.2014.10.021</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0041-0101(14)00352-3</ELocationID><Abstract><AbstractText>Ants (Hymenoptera: Formicidae) represent a taxonomically diverse group of arthropods comprising nearly 13,000 extant species. Sixteen ant subfamilies have individuals that possess a stinger and use their venom for purposes such as a defence against predators, competitors and microbial pathogens, for predation, as well as for social communication. They exhibit a range of activities including antimicrobial, haemolytic, cytolytic, paralytic, insecticidal and pain-producing pharmacologies. While ant venoms are known to be rich in alkaloids and hydrocarbons, ant venoms rich in peptides are becoming more common, yet remain understudied. Recent advances in mass spectrometry techniques have begun to reveal the true complexity of ant venom peptide composition. In the few venoms explored thus far, most peptide toxins appear to occur as small polycationic linear toxins, with antibacterial properties and insecticidal activity. Unlike other venomous animals, a number of ant venoms also contain a range of homodimeric and heterodimeric peptides with one or two interchain disulfide bonds possessing pore-forming, allergenic and paralytic actions. However, ant venoms seem to have only a small number of monomeric disulfide-linked peptides. The present review details the structure and pharmacology of known ant venom peptide toxins and their potential as a source of novel bioinsecticides and therapeutic agents.</AbstractText><CopyrightInformation>Copyright © 2014 Elsevier Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Aili</LastName><ForeName>Samira R</ForeName><Initials>SR</Initials><AffiliationInfo><Affiliation>Neurotoxin Research Group, School of Medical & Molecular Biosciences, University of Technology Sydney, NSW 2007, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Touchard</LastName><ForeName>Axel</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>CNRS, UMR Écologie des Forêts de Guyane (EcoFoG), Campus Agronomique, BP 316, 97379 Kourou Cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Escoubas</LastName><ForeName>Pierre</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>VenomeTech, 473 Route des Dolines - Villa 3, 06560 Valbonne, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Padula</LastName><ForeName>Matthew P</ForeName><Initials>MP</Initials><AffiliationInfo><Affiliation>Neurotoxin Research Group, School of Medical & Molecular Biosciences, University of Technology Sydney, NSW 2007, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Orivel</LastName><ForeName>Jérôme</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>CNRS, UMR Écologie des Forêts de Guyane (EcoFoG), Campus Agronomique, BP 316, 97379 Kourou Cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dejean</LastName><ForeName>Alain</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>CNRS, UMR Écologie des Forêts de Guyane (EcoFoG), Campus Agronomique, BP 316, 97379 Kourou Cedex, France; Laboratoire Écologie Fonctionnelle et Environnement, Université de Toulouse, 118 Route de Narbonne, 31062 Toulouse, France. Electronic address: alain.dejean@wanadoo.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nicholson</LastName><ForeName>Graham M</ForeName><Initials>GM</Initials><AffiliationInfo><Affiliation>Neurotoxin Research Group, School of Medical & Molecular Biosciences, University of Technology Sydney, NSW 2007, Australia. Electronic address: Graham.Nicholson@uts.edu.au.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>10</Month><Day>28</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Toxicon</MedlineTA><NlmUniqueID>1307333</NlmUniqueID><ISSNLinking>0041-0101</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000862">Ant Venoms</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000862" MajorTopicYN="N">Ant Venoms</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName><QualifierName UI="Q000145" MajorTopicYN="N">classification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001000" MajorTopicYN="N">Ants</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D044822" MajorTopicYN="Y">Biodiversity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005075" MajorTopicYN="Y">Biological Evolution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019281" MajorTopicYN="N">Dimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055808" MajorTopicYN="N">Drug Discovery</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013058" MajorTopicYN="N">Mass Spectrometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="Y">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000633" MajorTopicYN="Y">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017422" MajorTopicYN="N">Sequence Analysis, DNA</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013045" MajorTopicYN="N">Species Specificity</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Ant venom</Keyword><Keyword MajorTopicYN="N">Chemotaxonomy</Keyword><Keyword MajorTopicYN="N">Disulfide linkage</Keyword><Keyword MajorTopicYN="N">Peptides</Keyword><Keyword MajorTopicYN="N">Venom biochemistry</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>09</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>10</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>12</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>12</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>7</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25448389</ArticleId><ArticleId IdType="pii">S0041-0101(14)00352-3</ArticleId><ArticleId IdType="doi">10.1016/j.toxicon.2014.10.021</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Australie</li><li>France</li></country><region><li>Midi-Pyrénées</li><li>Occitanie (région administrative)</li></region><settlement><li>Toulouse</li></settlement></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="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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