Profiling the peptidome of the venom from the social wasp Agelaia pallipes pallipes

Baptista-Saidemberg, Nicoli B.; Saidemberg, Daniel Menezes; Palma, Mário Sérgio

doi:10.1016/j.jprot.2011.06.004

Cited by 28 publications

(28 citation statements)

References 32 publications

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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: 90%

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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Section: Linear Peptidessupporting

confidence: 90%

Diversity of peptide toxins from stinging ant venoms

Aili

Touchard

Escoubas³

et al. 2014

Toxicon

100

151

View full text Add to dashboard Cite

show abstract

“…Our computational method requires at least one template sequence as a reference. We investigated the membranolytic effects and membrane selectivities of two such templates: protonectin (ILGTILGLLKGL NH 2 ) [22,23] and decoralin (SLLSLIRKLIT NH 2 ), [24] two cationic AMPs from wasp venom. By computational design and residue permutation we generated variations of the template sequences and analyzed their effects with the aid of model lipid vesicles as membrane surrogates, surface plasmon resonance (SPR), isothermal titration calorimetry (ITC), circular dichroism (CD) spectroscopic measurements, and bacterial growth assays.…”

mentioning

confidence: 99%

Piloting the Membranolytic Activities of Peptides with a Self‐organizing Map

Lin¹,

Hiss²,

Schneider³

et al. 2014

ChemBioChem

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Antimicrobial peptides (AMPs) show remarkable selectivity toward lipid membranes and possess promising antibiotic potential. Their modes of action are diverse and not fully understood, and innovative peptide design strategies are needed to generate AMPs with improved properties. We present a de novo peptide design approach that resulted in new AMPs possessing low-nanomolar membranolytic activities. Thermal analysis revealed an entropy-driven mechanism of action. The study demonstrates sustained potential of advanced computational methods for designing peptides with the desired activity.

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“…The assignment of K/Q was further validated by first or second stage mass spectra of preand post-acetylation on the ε-amine groups of lysine residues [30], by using a MALDI-TOF/TOF mass spectrometer (ultraFlex, Bruker Daltonics, data not shown). Though the tolerance ±0.0180 Da is enough to distinguish K/Q, it is too relaxed to those ions in low mass.…”

Section: Sequence Determination and Primary Structure Analysismentioning

confidence: 99%

“…Therefore the former assignment was excluded (Supplemental Table S1 and S2, yellowed cell) by the ± 20 ppm limits. It is impossible to discriminate the isobaric I/L based on the data of the low energy CID MS/MS [17]; it could be achieved by the high energy collision-induced dissociation (HCD) MS/MS; however, the characteristic losses fragment ions (d or w ions) for the discrimination of I/L in HCD are not commonly observed [30,39,48,49]. Thus, it has been accepted to assign I/L indirectly based on the known sequences of the cDNA clones in the same species [29,50] or on the known sequences of analogues in the same or others species [39,48,49].…”

Section: Sequence Determination and Primary Structure Analysismentioning

confidence: 99%

“…As the molecular mass of the peptides increases, a large number of fragmentation pathways lead to a concomitant decrease in signal-tonoise ratio of the fragment ion peaks, which is the main reason that the observed second stage mass accuracy frequently exceeds the theoretical value [29]. Nonetheless, it could be alleviated by introducing the modified amino acid residues, such as acetylated K [30] or by employing the higher accuracy and resolution instruments, such as Orbitrap or FT-ICR MS [29]. Here, we described exact mass measurements that use low energy CID ESI Q-TOF MS/MS in positive-ion mode mass spectrometry, which is typically applied to de novo sequencing of peptides, to elucidate the mature AMPs components in crude venom sample from Odorrana jingdongensis.…”

Section: Introductionmentioning

confidence: 99%

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