Purification and chemical and biological characterizations of seven toxins from the Mexican scorpion, Centruroides suffusus suffusus.

Martin, Marie-Elise; Pérez, Leticia; Ayeb, Mohamed El; Kopeyan, Charles; Bechis, Guy; Jover, Emmanuel; Rochat, Hervé

doi:10.1016/s0021-9258(18)61214-1

Cited by 102 publications

(6 citation statements)

References 35 publications

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“…NaTx P01495* [17][18] Centruroides suffusus NaTx P08900* [19][20][21][22] Centruroides suffusus NaTx P60266* [23][24][25][26] Centruroides suffusus NaTx P0DL83* [21] Centruroides suffusus NaTx P60267…”

Section: Centruroides Noxiusmentioning

confidence: 99%

Phylogenomics of Scorpions Reveal Contemporaneous Diversification of Scorpion Mammalian Predators and Mammal-Active Sodium Channel Toxins

et al. 2022

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Scorpions constitute a charismatic lineage of arthropods and comprise more than 2500 described species. Found throughout various tropical and temperate habitats, these predatory arachnids have a long evolutionary history, with a fossil record that began in the Silurian. While all scorpions are venomous, the asymmetrically diverse family Buthidae harbors nearly half the diversity of extant scorpions, and all but one of the 58 species that are medically significant to humans. However, the lack of a densely sampled scorpion phylogeny has hindered broader inferences of the diversification dynamics of scorpion toxins. To redress this gap, we assembled a phylogenomic data set of 100 scorpion venom gland transcriptomes and genomes, emphasizing the sampling of highly toxic buthid genera. To infer divergence times of venom gene families, we applied a phylogenomic node dating approach for the species tree in tandem with phylostratigraphic bracketing to estimate the minimum ages of mammal-specific toxins. Our analyses establish a robustly supported phylogeny of scorpions, particularly with regard to relationships between medically significant taxa. Analysis of venom gene families shows that mammal-active sodium channel toxins (NaTx) have independently evolved in five lineages within Buthidae. Temporal windows of mammal-targeting toxin origins are correlated with the basal diversification of major scorpion mammal predators such as shrews, bats, and rodents. These results suggest an evolutionary model of relatively recent diversification of buthid NaTx homologs in response to the diversification of scorpion predators. [Adaptation; arachnids; phylogenomic dating; phylostratigraphy; venom.]

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Section: Centruroides Noxiusmentioning

confidence: 99%

Phylogenomics of Scorpions Reveal Contemporaneous Diversification of Scorpion Mammalian Predators and Mammal-Active Sodium Channel Toxins

et al. 2022

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“…Antimammalian β-toxins such as Cn2 and Css4 selectively target Na V channels of mammals. Cn2 isolated from Centruroides noxius is specific for Na V 1.6 channels, whereas Css4 isolated from Centruroides suffusus suffusus is sensitive to both Na V 1.6 and Na V 1.2 channels. , The two toxins share 83% sequence identity (Figure A). Antimammalian β-toxins bind to the periplasmic top of the VS domain of the II subunit of Na V channels and interfere with channel activation. ,− Following a transient depolarization voltage, the addition of β-toxins can cause sensitive Na V channels to open at less depolarized membrane potentials, leading to a left-shifted activity–voltage curve .…”

Section: Introductionmentioning

confidence: 99%

Conserved Functional Surface of Antimammalian Scorpion β-Toxins

Chen

Chung

2012

J. Phys. Chem. B

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Scorpion β-toxins bind to the voltage-sensing domain of voltage-gated sodium (NaV) channels and trap the voltage-sensing domain in the activated state. Two structurally similar β-toxins from scorpions, Css4 and Cn2, selectively target different subtypes of mammalian NaV channels. While the receptor site on the channels is known, the functional surface of the toxins remains to be understood. Here, we predict the binding modes of Css4 and Cn2 to the voltage-sensing domains of NaV1.2 and NaV1.6, respectively, with a molecular docking method and molecular dynamics simulations. The dissociation constants for the predicted toxin-channel complexes derived with umbrella sampling simulations are in accord with experiment. Our calculations suggest that the functional surface of Cn2 and Css4 is primarily formed by the loop between positions 8 and 18, centered on the two charged residues Lys13 and Glu15.

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“…The sequence CpoNatBet09 was 100% identical to the Cll2b toxin (UniProt P59899) from the C. limpidus; it presented identities of 89% and 86% with the toxins Css4 (UniProt P60266; C. suffusus) and Cn2 (UniProt P01495; C. noxius), respectively (Figure 4). These toxins are highly represented in their venoms, and present regions that are conserved in their amino acid sequences and are essential for their activity on sodium channels (L 39 , N 42 , Y 44 , R 47 , E 48 , Q 52 , W 78 ) [20,21]. In the case of the Cn2 toxin, it represents 6.8% of the total venom, with an LD 50 of 0.25 µg/20 g of the mouse to which it was administered intraperitoneally [22,23].…”

Section: Ion Channel-acting Toxinsmentioning

confidence: 99%

Unveiling the Protein Components of the Secretory-Venom Gland and Venom of the Scorpion Centruroides possanii (Buthidae) through Omic Technologies

García-Villalvazo

Jiménez-Vargas

Lino-López³

et al. 2023

Toxins

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Centruroides possanii is a recently discovered species of “striped scorpion” found in Mexico. Certain species of Centruroides are known to be toxic to mammals, leading to numerous cases of human intoxications in the country. Venom components are thought to possess therapeutic potential and/or biotechnological applications. Hence, obtaining and analyzing the secretory gland transcriptome and venom proteome of C. possanii is relevant, and that is what is described in this communication. Since this is a newly described species, first, its LD50 to mice was determined and estimated to be 659 ng/g mouse weight. Using RNA extracted from this species and preparing their corresponding cDNA fragments, a transcriptome analysis was obtained on a Genome Analyzer (Illumina) using the 76-base pair-end sequencing protocol. Via high-throughput sequencing, 19,158,736 reads were obtained and ensembled in 835,204 sequences. Of them, 28,399 transcripts were annotated with Pfam. A total of 244 complete transcripts were identified in the transcriptome of C. possanii. Of these, 109 sequences showed identity to toxins that act on ion channels, 47 enzymes, 17 protease inhibitors (PINs), 11 defense peptides (HDPs), and 60 in other components. In addition, a sample of the soluble venom obtained from this scorpion was analyzed using an Orbitrap Velos apparatus, which allowed for identification by liquid chromatography followed by mass spectrometry (LC-MS/MS) of 70 peptides and proteins: 23 toxins, 27 enzymes, 6 PINs, 3 HDPs, and 11 other components. Until now, this work has the highest number of scorpion venom components identified through omics technologies. The main novel findings described here were analyzed in comparison with the known data from the literature, and this process permitted some new insights in this field.

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Purification and chemical and biological characterizations of seven toxins from the Mexican scorpion, Centruroides suffusus suffusus.

Cited by 102 publications

References 35 publications

Phylogenomics of Scorpions Reveal Contemporaneous Diversification of Scorpion Mammalian Predators and Mammal-Active Sodium Channel Toxins

Phylogenomics of Scorpions Reveal Contemporaneous Diversification of Scorpion Mammalian Predators and Mammal-Active Sodium Channel Toxins

Conserved Functional Surface of Antimammalian Scorpion β-Toxins

Unveiling the Protein Components of the Secretory-Venom Gland and Venom of the Scorpion Centruroides possanii (Buthidae) through Omic Technologies

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