A New Family of Small (4kDa) Neurotoxins from the Venoms of Spiders of the Genus Phoneutria

Lucio, A. D.; Campos, Fabiana V.; Richardson, Michael; Cordeiro, Marta N.; Mazzoni, Mário S. C.; Lima, M.E. de; Pimenta, Adriano M.C.; Bemquerer, Marcelo P.; Figueiredo, Suely G.; Gomes, Paulo César; Beirão, Paulo Sérgio Lacerda

doi:10.2174/092986608785133708

Cited by 10 publications

(3 citation statements)

References 40 publications

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“…Toxins PRTx26An0C3 (UniProt: P86418) and U4-ctenitoxin-Pr1a (UniProt: P83892) can cause spastic paralysis and death in mice and are moderate inhibitors of L-Cav1/CACNA1 type calcium channels. On the other hand, toxin U6-ctenitoxin-Pk1a (UniProt: P83910), despite causing spastic paralysis and death in mice, has no detectable action on those channels [ 73 ]. In contrast, toxins U23-ctenitoxin-Pn1a (UniProt: P84015) and U13-ctenitoxin (UniProt: P83894) have no toxic effect on mice.…”

Section: Resultsmentioning

confidence: 99%

An overview of Phoneutria nigriventer spider venom using combined transcriptomic and proteomic approaches

et al. 2018

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Phoneutria nigriventer is one of the largest existing true spiders and one of the few considered medically relevant. Its venom contains several neurotoxic peptides that act on different ion channels and chemical receptors of vertebrates and invertebrates. Some of these venom toxins have been shown as promising models for pharmaceutical or biotechnological use. However, the large diversity and the predominance of low molecular weight toxins in this venom have hampered the identification and deep investigation of the less abundant toxins and the proteins with high molecular weight. Here, we combined conventional and next-generation cDNA sequencing with Multidimensional Protein Identification Technology (MudPIT), to obtain an in-depth panorama of the composition of P. nigriventer spider venom. The results from these three approaches showed that cysteine-rich peptide toxins are the most abundant components in this venom and most of them contain the Inhibitor Cysteine Knot (ICK) structural motif. Ninety-eight sequences corresponding to cysteine-rich peptide toxins were identified by the three methodologies and many of them were considered as putative novel toxins, due to the low similarity to previously described toxins. Furthermore, using next-generation sequencing we identified families of several other classes of toxins, including CAPs (Cysteine Rich Secretory Protein—CRiSP, antigen 5 and Pathogenesis-Related 1—PR-1), serine proteinases, TCTPs (translationally controlled tumor proteins), proteinase inhibitors, metalloproteinases and hyaluronidases, which have been poorly described for this venom. This study provides an overview of the molecular diversity of P. nigriventer venom, revealing several novel components and providing a better basis to understand its toxicity and pharmacological activities.

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Section: Resultsmentioning

confidence: 99%

An overview of Phoneutria nigriventer spider venom using combined transcriptomic and proteomic approaches

et al. 2018

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“…The new procedure also resulted in the discovery of two new structural families of Phoneutria peptides (Penaforte et al, 2000;Richardson et al, 2006). The family of 4 kDa toxins targets Cav channels (Lucio et al, 2008). Two different isoforms PnTx27C4 and PnTx26AN0C3 were isolated and characterized.…”

Section: Phtx5mentioning

confidence: 99%

Phoneutria nigriventer venom: A pharmacological treasure

Peigneur

Lima

Tytgat

2018

Toxicon

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“…Except for other sequences from Scytodes thoracica , no sequences matched U 3 -Sth1a or U 3 -Sth1h with expect values less than 10 −5 (a commonly used threshold for sequence homology; [ 37 ]). For example, the closest match for U 3 -Sth1a from another species was U 4 -ctenitoxin-Pr1a, a peptide from the venom of the spider Phoneutria reidyi that moderately inhibits L-type voltage-gated calcium channels (Ca V 1/CACNA1) [ 38 ] matched with an expect value of 0.009. For U 3 -Sth1h, the closest match from another species was U 21 -ctenitoxin-Co1a from the venom of the spider Ctenus ornatus which has an unknown molecular target [ 4 ], with an expect value of 0.016.…”

Section: Resultsmentioning

confidence: 99%

Characterization of Three Venom Peptides from the Spitting Spider Scytodes thoracica

Ariki¹,

Muñoz²,

Armitage³

et al. 2016

PLoS ONE

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We present the solution-state NMR structures and preliminary functional characterizations of three venom peptides identified from the spitting spider Scytodes thoracica. Despite little sequence identity to other venom peptides, structural characterization reveals that these peptides contain an inhibitor cystine knot motif common to many venom peptides. These are the first structures for any peptide or protein from spiders of the Scytodidae family. Many venom peptides target neuronal ion channels or receptors. However, we have not been able to determine the target of these Scytodes peptides so we can only state with certainty the channels and receptors that they do not target.

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A New Family of Small (4kDa) Neurotoxins from the Venoms of Spiders of the Genus Phoneutria

Cited by 10 publications

References 40 publications

An overview of Phoneutria nigriventer spider venom using combined transcriptomic and proteomic approaches

An overview of Phoneutria nigriventer spider venom using combined transcriptomic and proteomic approaches

Phoneutria nigriventer venom: A pharmacological treasure

Characterization of Three Venom Peptides from the Spitting Spider Scytodes thoracica

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