Brown Recluse Spider Venom: Proteomic Analysis and Proposal of a Putative Mechanism of Action

Santos, Lucilene Delazari dos; Dias, Nathalia Baptista; Roberto, José; Pinto, Artur Soares; Palma, Mário Sérgio

doi:10.2174/092986609788923383

Cited by 38 publications

(35 citation statements)

References 60 publications

(67 reference statements)

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“…Allergens/Lipocalins have been identified as potential toxins in spider venoms, which are potent molecules to cause sensitization and disrupt hemostasis [29,46,54,55,56]. Data from our present work showed that 11 unigenes in the L. tredecimguttatus eggs encoded allergens/lipocalins (Table S3).…”

Section: Resultsmentioning

confidence: 60%

Transcriptome Analysis to Understand the Toxicity of Latrodectus tredecimguttatus Eggs

Wang

2016

Toxins

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Latrodectus tredecimguttatus is a kind of highly venomous black widow spider, with toxicity coming from not only venomous glands but also other parts of its body as well as newborn spiderlings and eggs. Up to date, although L. tredecimguttatus eggs have been demonstrated to be rich in proteinaceous toxins, there is no systematic investigation on such active components at transcriptome level. In this study, we performed a high-throughput transcriptome sequencing of L. tredecimguttatus eggs with Illumina sequencing technology. As a result, 53,284 protein-coding unigenes were identified, of which 14,185 unigenes produced significant hits in the available databases, including 280 unigenes encoding proteins or peptides homologous to known proteinaceous toxins. GO term and KEGG pathway enrichment analyses of the 280 unigenes showed that 375 GO terms and 18 KEGG pathways were significantly enriched. Functional analysis indicated that these unigene-coded toxins have the bioactivities to degrade tissue proteins, inhibit ion channels, block neuromuscular transmission, provoke anaphylaxis, induce apoptosis and hyperalgesia, etc. No known typical proteinaceous toxins in L. tredecimguttatus venomous glands, such as latrotoxins, were identified, suggesting that the eggs have a different toxicity mechanism from that of the venom. Our present transcriptome analysis not only helps to reveal the gene expression profile and toxicity mechanism of the L. tredecimguttatus eggs, but also provides references for the further related researches.

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Section: Resultsmentioning

confidence: 60%

Transcriptome Analysis to Understand the Toxicity of Latrodectus tredecimguttatus Eggs

Wang

2016

Toxins

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“…Since the searches retrieved no significant match, de novo sequencing was performed and the resulting sequences were BLASTed against the non-redundant sequences, allowing SMD identification for all analyzed spots 22 . Only in 2009 was a proteomic study described that targeted the total protein content of the Loxosceles venom 23 . Although the L. intermedia venom was analyzed using Multi-Dimensional Protein Identification Technology (MudPIT) 24 , only 39 proteins were identified.…”

Section: Background and Summarymentioning

confidence: 99%

“…Although the L. intermedia venom was analyzed using Multi-Dimensional Protein Identification Technology (MudPIT) 24 , only 39 proteins were identified. Of these proteins, only 14 were described as toxins generally found in animal venoms 23 . Thus, this proteomic study seems to have severely underestimated the great toxin diversity of the Loxosceles venom, particularly in comparison to the many publications that already described distinct molecular clones from venoms of different Loxosceles species 25–32 .…”

Section: Background and Summarymentioning

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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“…amnh.org/iz/spiders/catalog/COUNTS.html). Spiders roam the world and have conquered most terrestrial environments (Dos Santos et al, 2009;Hu et al, 2014). One of the major contributors to the evolutionary success of spiders is their ability to produce complex venoms for predation and predator deterrence (King, 2004).…”

Section: Introductionmentioning

confidence: 99%

A survey of the venom of the spider Lycosa vittata by biochemical, pharmacological and transcriptomic analyses

Zhang

Liu

Tan

et al. 2015

Toxicon

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Lycosa vittata, mainly distributed in the southwest of China, is a medium-sized and venomous spider, whose venom remains unexplored so far. This study aims to present an overview of the venom. It mainly consisted of diverse peptides and exhibited inhibitory effects on voltage-gated ion channels in rat dorsal root ganglia neurons, with a strongest inhibition on tetrodotoxin-sensitive and tetrodotoxin-resistant voltage-gated Na(+) channels. Interestingly, it exerted cytotoxicity to cancer cells, with approximately 10-fold selectivity on PC-3 over others, implying the existence of selective anti-PC-3 agents in the venom. Moreover, 51 toxin-like peptides were deduced from the venom gland transcriptome. Bioinformatic analyses suggested their structures might have some distinguished properties and their predicted functions were consistent with the venom activities. This study suggests that the venom is an attractive source of neurotoxins with therapeutic significance, and provides references for the structure and function investigation of specific toxins in the future.

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Brown Recluse Spider Venom: Proteomic Analysis and Proposal of a Putative Mechanism of Action

Cited by 38 publications

References 60 publications

Transcriptome Analysis to Understand the Toxicity of Latrodectus tredecimguttatus Eggs

Transcriptome Analysis to Understand the Toxicity of Latrodectus tredecimguttatus Eggs

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

A survey of the venom of the spider Lycosa vittata by biochemical, pharmacological and transcriptomic analyses

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