Diversity of peptide toxins from stinging ant venoms.
Identifieur interne : 003A21 ( Main/Exploration ); précédent : 003A20; suivant : 003A22Diversity 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
Affiliations:
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<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>
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<term>Molecular Sequence Data</term>
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<term>Peptides (toxicity)</term>
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<term>Sequence Analysis, DNA</term>
<term>Species Specificity</term>
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<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>
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<term>Dimerization</term>
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<term>Molecular Sequence Data</term>
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<term>Données de séquences moléculaires</term>
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<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>
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