Differential metalloprotease content and activity of three Loxosceles spider venoms revealed using two-dimensional electrophoresis approaches

Trevisan-Silva, Dilza; Bednaski, Aline Viana; Gremski, Luiza Helena; Chaim, Olga Meiri; Veiga, Sílvio Sanches; Senff‐Ribeiro, Andrea

doi:10.1016/j.toxicon.2013.08.065

Cited by 23 publications

(21 citation statements)

References 49 publications

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“…28) and only later recognized as a family of toxins present in the Loxosceles venom 33 . These toxins present proteolytic activity on distinct extracellular matrix proteins and are related to the hemostatic effects in loxoscelism 43,49 .…”

Section: Technical Validationmentioning

confidence: 99%

A multi-protease, multi-dissociation, bottom-up-to-top-down proteomic view of the Loxosceles intermedia venom

et al. 2017

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Venoms are a rich source for the discovery of molecules with biotechnological applications, but their analysis is challenging even for state-of-the-art proteomics. Here we report on a large-scale proteomic assessment of the venom of Loxosceles intermedia, the so-called brown spider. Venom was extracted from 200 spiders and fractioned into two aliquots relative to a 10 kDa cutoff mass. Each of these was further fractioned and digested with trypsin (4 h), trypsin (18 h), pepsin (18 h), and chymotrypsin (18 h), then analyzed by MudPIT on an LTQ-Orbitrap XL ETD mass spectrometer fragmenting precursors by CID, HCD, and ETD. Aliquots of undigested samples were also analyzed. Our experimental design allowed us to apply spectral networks, thus enabling us to obtain meta-contig assemblies, and consequently de novo sequencing of practically complete proteins, culminating in a deep proteome assessment of the venom. Data are available via ProteomeXchange, with identifier PXD005523.

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Section: Technical Validationmentioning

confidence: 99%

A multi-protease, multi-dissociation, bottom-up-to-top-down proteomic view of the Loxosceles intermedia venom

et al. 2017

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“…LiTCTP could also facilitate the diffusion of other toxins, ultimately promoting venom components spreading from the bite site. Other brown spider toxins that promote extracellular matrix degradation and remodeling, such as metalloproteinases and hyaluronidases, are also implicated in this process [8,52,53]. This combined effect of LiRecDT1 and LiRecTCTP was reproduced in the Evans blue assay.…”

Section: Discussionmentioning

confidence: 90%

TCTP from Loxosceles Intermedia (Brown Spider) Venom Contributes to the Allergic and Inflammatory Response of Cutaneous Loxoscelism

Bóia-Ferreira

Moreno

Basílio

et al. 2019

Cells

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LiTCTP is a toxin from the Translationally Controlled Tumor Protein (TCTP) family identified in Loxosceles brown spider venoms. These proteins are known as histamine-releasing factors (HRF). TCTPs participate in allergic and anaphylactic reactions, which suggest their potential role as therapeutic targets. The histaminergic effect of TCTP is related to its pro-inflammatory functions. An initial characterization of LiTCTP in animal models showed that this toxin can increase the microvascular permeability of skin vessels and induce paw edema in a dose-dependent manner. We evaluated the role of LiTCTP in vitro and in vivo in the inflammatory and allergic aspects that undergo the biological responses observed in Loxoscelism, the clinical condition after an accident with Loxosceles spiders. Our results showed LiTCTP recombinant toxin (LiRecTCTP) as an essential synergistic factor for the dermonecrotic toxin actions (LiRecDT1, known as the main toxin in the pathophysiology of Loxoscelism), revealing its contribution to the exacerbated inflammatory response clinically observed in envenomated patients.

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“…All of the sequences we detect have the conserved catalytic domain HEXXHXXGXXHEXXRXDR-and a MXY region that is involved with a sequence turn and Zn-dependent activity (da Silveira et al, 2007). LALPs have proteolytic effects on gelatin, fibronectin, fibrinogen and extracellular matrices, and thus, as venom toxins, they are hypothesized to be spreading factors that act in synergy with other toxins (Trevisan-Silva et al, 2013). FIGURE 3 | A Bayesian phylogeny of astacin metalloproteinases (M12 peptidases) supports evolutionary expansion in the venom of male Physocyclus mexicanus.…”

Section: Astacin Metalloproteinases (M12 Peptidases)mentioning

confidence: 99%

“…The hydrolytic effects of LALPs are suspected to contribute to hemostatic disturbance during mammalian envenomation, thereby influencing the dermonecrotic or systemic effects of Loxosceles bites (Trevisan-Silva et al, 2013).…”

Section: Astacin Metalloproteinases (M12 Peptidases)mentioning

confidence: 99%

Not so Dangerous After All? Venom Composition and Potency of the Pholcid (Daddy Long-Leg) Spider Physocyclus mexicanus

Zobel-Thropp

Mullins

Kristensen³

et al. 2019

Front. Ecol. Evol.

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Pholcid spiders (Araneae: Pholcidae), officially "cellar spiders" but popularly known as "daddy long-legs," are renown for the potential of deadly toxic venom, even though venom composition and potency has never formally been studied. Here we detail the venom composition of male Physocyclus mexicanus using proteomic analyses and venom-gland transcriptomes ("venomics"). We also analyze the venom's potency on insects, and assemble available evidence regarding mammalian toxicity. The majority of the venom (51% of tryptic polypeptides and 62% of unique tryptic peptides) consists of proteins homologous to known venom toxins including enzymes (astacin metalloproteases, serine proteases and metalloendopeptidases, particularly neprilysins) and venom peptide neurotoxins. We identify 17 new groups of peptides (U 1−17-PHTX) most of which are homologs of known venom peptides and are predicted to have an inhibitor cysteine knot fold; of these, 13 are confirmed in the proteome. Neprilysins (M13 peptidases), and astacins (M12 peptidases) are the most abundant venom proteins, respectively representing 15 and 11% of the individual proteins and 32 and 20% of the tryptic peptides detected in crude venom. Comparative evidence suggests that the neprilysin gene family is expressed in venoms across a range of spider taxa, but has undergone an expansion in the venoms of pholcids and may play a central functional role in these spiders. Bioassays of crude venoms on crickets resulted in an effective paralytic dose of 3.9 µg/g, which is comparable to that of crude venoms of Plectreurys tristis and other Synspermiata taxa. However, crickets exhibit flaccid paralysis and regions of darkening that are not observed after P. tristis envenomation. Documented bites on humans make clear that while these spiders can bite, the typical result is a mild sting with no long-lasting effects. Together, the evidence we present indicates pholcid venoms are a source of interesting new peptides and proteins, and effects of bites on humans and other mammals are inconsequential.

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Differential metalloprotease content and activity of three Loxosceles spider venoms revealed using two-dimensional electrophoresis approaches

Cited by 23 publications

References 49 publications

A multi-protease, multi-dissociation, bottom-up-to-top-down proteomic view of the Loxosceles intermedia venom

A multi-protease, multi-dissociation, bottom-up-to-top-down proteomic view of the Loxosceles intermedia venom

TCTP from Loxosceles Intermedia (Brown Spider) Venom Contributes to the Allergic and Inflammatory Response of Cutaneous Loxoscelism

Not so Dangerous After All? Venom Composition and Potency of the Pholcid (Daddy Long-Leg) Spider Physocyclus mexicanus

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