The diversity of venom components of the scorpion species Paravaejovis schwenkmeyeri (Scorpiones: Vaejovidae) revealed by transcriptome and proteome analyses

Cid-Uribe, Jimena I.; Santibáñez‐López, Carlos E.; Meneses, Erika P.; Batista, Cesar Vicente Ferreira; Jiménez-Vargas, Juana María; Ortíz, Ernesto; Possani, L.D.

doi:10.1016/j.toxicon.2018.06.085

Cited by 34 publications

(45 citation statements)

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“…This has been documented in previous proteomic and transcriptomic analyses. The toxic fraction in most buthids is high (ranging from 66% to 85% of the venomous peptides reported [ 13 , 14 , 15 , 16 ]), while in non-buthid scorpions, it is much lower (from 9% to 20% [ 8 , 9 , 14 , 17 , 18 , 19 , 20 ]).…”

Section: Resultsmentioning

confidence: 99%

“…Given the above, and that S. gertschi is a non-buthid species, it came as a surprise that the subgroup of transcripts potentially coding for ion channel toxins was the most diverse in the transcriptome by a significant extent (31.2% of all transcripts, see Figure 2 ). In previous high-throughput analyses of non-buthid species, this subgroup was either outnumbered by other venom components (as in T. atrox and M. gertschi , for which enzymes were the most diverse [ 8 , 18 ]) or on par with those other components (as in Superstitionia donensis and P. schwenkmeyeri [ 9 , 19 ]. The reason for this observation remains to be determined.…”

Section: Resultsmentioning

confidence: 99%

“…These studies showed that the biodiversity of NDBPs was high in these species’ venoms. More recently, the first high-throughput transcriptomic and proteomic analyses for the Vaejovidae species were performed for T. atrox [ 8 ] and Paravaejovis schwenkmeyeri [ 9 ], suggesting that the diversity of the ion channel toxin components found in previous studies is similar. Unfortunately, the Vaejovidae family is among the most diverse scorpion families, and the diversity of venom components is known only from a handful of species restricted to two (of three) subfamilies and four (out of 25) genera included in this family, preventing further studies on venom evolution.…”

Section: Introductionmentioning

confidence: 96%

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Transcriptomic and Proteomic Analyses Reveal the Diversity of Venom Components from the Vaejovid Scorpion Serradigitus gertschi

Romero-Gutiérrez

Santibáñez‐López

Jiménez-Vargas

et al. 2018

Toxins

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To understand the diversity of scorpion venom, RNA from venomous glands from a sawfinger scorpion, Serradigitus gertschi, of the family Vaejovidae, was extracted and used for transcriptomic analysis. A total of 84,835 transcripts were assembled after Illumina sequencing. From those, 119 transcripts were annotated and found to putatively code for peptides or proteins that share sequence similarities with the previously reported venom components of other species. In accordance with sequence similarity, the transcripts were classified as potentially coding for 37 ion channel toxins; 17 host defense peptides; 28 enzymes, including phospholipases, hyaluronidases, metalloproteases, and serine proteases; nine protease inhibitor-like peptides; 10 peptides of the cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 protein superfamily; seven La1-like peptides; and 11 sequences classified as “other venom components”. A mass fingerprint performed by mass spectrometry identified 204 components with molecular masses varying from 444.26 Da to 12,432.80 Da, plus several higher molecular weight proteins whose precise masses were not determined. The LC-MS/MS analysis of a tryptic digestion of the soluble venom resulted in the de novo determination of 16,840 peptide sequences, 24 of which matched sequences predicted from the translated transcriptome. The database presented here increases our general knowledge of the biodiversity of venom components from neglected non-buthid scorpions.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 96%

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Transcriptomic and Proteomic Analyses Reveal the Diversity of Venom Components from the Vaejovid Scorpion Serradigitus gertschi

Romero-Gutiérrez

Santibáñez‐López

Jiménez-Vargas

et al. 2018

Toxins

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“…Scorpion venoms are cocktails of diverse biologically active compounds (see, inter alia, Rodriguez de la Vega and Possani, 2005;Rodriguez de la Vega et al 2010;Cao et al 2014;Abdel-Rahman et al 2015;Cid-Uribe et al 2018;Kazemi and Sabatier, 2019) and provide a rich source of AMPs (for reviews see Harrison et al 2014;Wang and Wang, 2016;El-Bitar et al 2019). Abdel-Rahman et al (2013) identified two novel amphipathic cationic AMPs (Smp43 and Smp24) through cDNA sequencing of the venom gland of the Egyptian scorpion Scorpio maurus palmatus.…”

Section: Introductionmentioning

confidence: 99%

Cytotoxic Effects of Smp24 and Smp43 Scorpion Venom Antimicrobial Peptides on Tumour and Non-tumour Cell Lines

Elrayess

Mohallal

El-Shahat

et al. 2019

Int J Pept Res Ther

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Smp24 and Smp43 are novel cationic AMPs identified from the venom of the Egyptian scorpion Scorpio maurus palmatus, having potent activity against both Gram-positive and Gram-negative bacteria as well as fungi. Here we describe cytotoxicity of these peptides towards three non-tumour cell lines (CD34 + (hematopoietic stem progenitor from cord blood), HRECs (human renal epithelial cells) and HACAT (human skin keratinocytes) and two acute leukaemia cell lines (myeloid (KG1a) and lymphoid (CCRF-CEM) leukaemia cell lines) using a combination of biochemical and imaging techniques. Smp24 and Smp43 (4-256 µg/mL) decreased the cell viability (as measured by intracellular ATP) of all cells tested, although keratinocytes were markedly less sensitive. Cell membrane leakage as evidenced by the release of lactate dehydrogenase was evident throughout and was confirmed by scanning electron microscope studies.

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“…transcriptomic study of a non-buthid scorpion belonging to the family Vaejovidae (Cid-Uribe et al, 2018) and Ward et al examines sex-related differences in the venom composition of the Hentz striped scorpion (Ward et al, 2018a). The remaining reviews do not focus on specific arthropod lineages, but rather provide a general overview of the biochemistry and evolution of arthropod venoms (Laxme et al, 2018) or the structural diversity of arthropod toxins (Daly and Wilson, 2018).…”

Section: Content Of This Special Toxicon Issue On Arthropod Venomsmentioning

confidence: 99%

Arthropod assassins: Crawling biochemists with diverse toxin pharmacopeias

Herzig

2019

Toxicon

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The millions of extant arthropod species are testament to their evolutionary success that can at least partially be attributed to venom usage, which evolved independently in at least arthropod lineages. While some arthropods primarily use venom for predation (e.g., spiders and centipedes) or defense (e.g., bees and caterpillars), it can also have more specialised functions (e.g. in parasitoid wasps to paralyse arthropods for their brood to feed on) or even a combination of functions (e.g. the scorpion Parabuthus transvaalicus can deliver a prevenom for predator deterrence and a venom for predation). Most arthropod venoms are complex cocktails of water, salts, small bioactive molecules, peptides, enzymes and larger proteins, with peptides usually comprising the majority of toxins. Some spider venoms have been reported to contain > 1,000 peptide toxins, which function as combinatorial libraries to provide an evolutionary advantage. The astounding diversity of venomous arthropods multiplied by their enormous toxin arsenals results in an almost infinite resource for novel bioactive molecules. The main challenge for exploiting this resource is the small size of most arthropods, which can be a limitation for current venom extraction techniques. Fortunately, recent decades have seen an incredible improvement in transcriptomic and proteomic techniques that have provided increasing sensitivity while reducing sample requirements. In turn, this has provided a much larger variety of arthropod venom compounds for potential applications such as therapeutics, molecular probes for basic research, bioinsecticides or anti-parasitic drugs. This special issue of Toxicon aims to cover the breadth of arthropod venom research, including toxin evolution, pharmacology, toxin discovery and characterisation, toxin structures, clinical aspects, and potential applications. 1. Diversity of arthropod venom systems

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The diversity of venom components of the scorpion species Paravaejovis schwenkmeyeri (Scorpiones: Vaejovidae) revealed by transcriptome and proteome analyses

Cited by 34 publications

References 110 publications

Transcriptomic and Proteomic Analyses Reveal the Diversity of Venom Components from the Vaejovid Scorpion Serradigitus gertschi

Transcriptomic and Proteomic Analyses Reveal the Diversity of Venom Components from the Vaejovid Scorpion Serradigitus gertschi

Cytotoxic Effects of Smp24 and Smp43 Scorpion Venom Antimicrobial Peptides on Tumour and Non-tumour Cell Lines

Arthropod assassins: Crawling biochemists with diverse toxin pharmacopeias

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