Structure–function relationships of the peptide Paulistine: A novel toxin from the venom of the social wasp Polybia paulista

Gomes, Paulo César; Souza, Bibiana Monson de; Dias, Nathalia Baptista; Brigatte, Patrícia; Mourelle, Danilo; Arcuri, Helen Andrade; Cabrera, Marcia Perez dos Santos; Stábeli, Rodrigo G.; Neto, João Ruggiero; Palma, Mário Sérgio

doi:10.1016/j.bbagen.2013.08.024

Cited by 14 publications

(11 citation statements)

References 40 publications

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“…By combining MALDI-TOF MS with chromatographic separation, we have shown that the Odontomachus haematodus venom peptidome is composed of more than 100 small and linear peptides in the 700-3000 m/z mass range. This feature is consistent with a previous study on the venoms of five Neotropical Odontomachus species as well as wasp and cone snail venoms which are usually comprised of peptides with fewer than 35 residues (Baptista-Saidemberg et al 2011; Cologna et al 2013;de Souza et al 2004;Gomes et al 2014;Johnson et al 2010;Lewis et al 2012;Orivel et al 2001). In contrast, spider, scorpion and snake venoms may also contain larger peptides with typically from 30 to 100 amino acids (Olivera et al 1990).…”

Section: Discussionsupporting

confidence: 91%

Intraspecific variations in the venom peptidome of the ant Odontomachus haematodus (Formicidae: Ponerinae) from French Guiana

Touchard¹,

Déjean²,

Escoubas³

et al. 2015

JHR

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Ant venoms are complex cocktails of toxins employed to subdue prey and to protect the colony from predators and microbial pathogens. Although the extent of ant venom peptide diversity remains largely unexplored, previous studies have revealed the presence of numerous bioactive peptides in most stinging ant venoms. We investigated the venom peptidome of the ponerine ant Odontomachus haematodus using LC-MS analysis and then verified whether the division of labor in the colonies and their geographical location are correlated with differences in venom composition. Our results reveal that O. haematodus venom is comprised of 105 small linear peptides. The venom composition does not vary between the different castes (i.e., nurses, foragers and queens), but an intraspecific variation in peptide content was observed, particularly when the colonies are separated by large distances. Geographical variation appears to increase the venom peptide repertoire of this ant species, demonstrating its intraspecific venom plasticity.

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Section: Discussionsupporting

confidence: 91%

Intraspecific variations in the venom peptidome of the ant Odontomachus haematodus (Formicidae: Ponerinae) from French Guiana

Touchard¹,

Déjean²,

Escoubas³

et al. 2015

JHR

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“…This is consistent with studies performed on other hymenopteran (wasp and bee) venoms (Argiolas and Pisano, 1985;Baptista-Saidemberg et al, 2011;Dias et al, 2014;Favreau et al, 2006;Gomes et al, 2014;Mendes et al, 2004;Qiu et al, 2012). Many of these linear peptides have antimicrobial properties and some possess additional insecticidal activity.…”

Section: Linear Peptidessupporting

confidence: 89%

Diversity of peptide toxins from stinging ant venoms

Aili

Touchard

Escoubas³

et al. 2014

Toxicon

100

151

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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.

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“…[58] Hymenopteran venom peptides have not been extensively investigated to date. However, past studies on wasp venoms revealed small linear peptides [14,[59][60][61] and some rare single disulfide-linked peptides such as pallipine-I, ÀII and -III from the venom of the wasp Agelaia p. pallipes [14] and sylverin from the venom of Protonectarina sylveirae. [62] A wide survey of ant venom peptidomes has never been attempted before and this study therefore constitutes the most extensive overview conducted to date, providing a broad overview of the variability of ant venom peptide composition.…”

Section: Discussionmentioning

confidence: 99%

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

Touchard

Koh

Aili

et al. 2015

Rapid Comm Mass Spectrometry

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Structure–function relationships of the peptide Paulistine: A novel toxin from the venom of the social wasp Polybia paulista

Abstract: The peptides Paulistine and Acm-Paulistine may be used as interesting tools to investigate the mechanisms of pain and inflammation in future studies.

Cited by 14 publications

References 40 publications

Intraspecific variations in the venom peptidome of the ant Odontomachus haematodus (Formicidae: Ponerinae) from French Guiana

Intraspecific variations in the venom peptidome of the ant Odontomachus haematodus (Formicidae: Ponerinae) from French Guiana

Diversity of peptide toxins from stinging ant venoms

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

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