Venom proteomic and venomous glands transcriptomic analysis of the Egyptian scorpion Scorpio maurus palmatus (Arachnida: Scorpionidae)

Abdel-Rahman, Mohamed A.; Quintero-Hernández, Verónica; Possani, Lourival D.

doi:10.1016/j.toxicon.2013.08.064

Cited by 82 publications

(69 citation statements)

References 82 publications

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“…Butantoxin, on the other hand, is a potassium channel blocker purified from T. serrulatus, T. bahiensis and T. stigmurus (Holaday et al, 2000). Peptides and enzymatic proteins present in the composition of the venom from some scorpion species have been investigated by different approaches such as transcriptomic and proteomic methods (Kalapothakis et al, 2001;Pimenta et al, 2001;Goudet et al, 2002;Schwartz et al, 2007;Ma et al, 2009Ma et al, , 2010Ruiming et al, 2010;Morgenstern et al, 2011;D'Suze et al, 2009;Batista et al, 2006Batista et al, , 2007Bringans et al, 2008;Rates et al, 2008;Ma et al, 2012;Diego-Garcia et al, 2012;Almeida et al, 2012;Alvarenga et al, 2012;Rend on-Anaya et al, 2012;Abdel-Rahman et al, 2013;He et al, 2013;Luna-Ramírez et al, 2013;Valdez-Vel azquez et al, 2013). However, no large-scale effort has been carried out for T. bahiensis and only a few reports of sequencing specific toxins are found in the literature (Becerril et al, 1996(Becerril et al, , 1997Trequattrini et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

The transcriptome recipe for the venom cocktail of Tityus bahiensis scorpion

Oliveira

Cândido

Dorce

et al. 2015

Toxicon

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Scorpion venom is a mixture of peptides, including antimicrobial, bradykinin-potentiating and anionic peptides and small to medium proteins, such as ion channel toxins, metalloproteinases and phospholipases that together cause severe clinical manifestation. Tityus bahiensis is the second most medically important scorpion species in Brazil and it is widely distributed in the country with the exception of the North Region. Here we sequenced and analyzed the transcripts from the venom glands of T. bahiensis, aiming at identifying and annotating venom gland expressed genes. A total of 116,027 long reads were generated by pyrosequencing and assembled in 2891 isotigs. An annotation process identified transcripts by similarity to known toxins, revealing that putative venom components represent 7.4% of gene expression. The major toxins identified are potassium and sodium channel toxins, whereas metalloproteinases showed an unexpected high abundance. Phylogenetic analysis of deduced metalloproteinases from T. bahiensis and other scorpions revealed a pattern of ancient and intraspecific gene expansions. Other venom molecules identified include antimicrobial, anionic and bradykinin-potentiating peptides, besides several putative new venom components. This report provides the first attempt to massively identify the venom components of this species and constitutes one of the few transcriptomic efforts on the genus Tityus.

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Section: Introductionmentioning

confidence: 99%

The transcriptome recipe for the venom cocktail of Tityus bahiensis scorpion

Oliveira

Cândido

Dorce

et al. 2015

Toxicon

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“…The soluble venom was centrifuged at 14,000 rpm for 10 min at 4°C. The supernatant was pooled; freeze dried (Labconco Freeze Dry System, Kansas, USA) and the stock was stored at À20°C until use (Abdel-Rahman et al, 2013). The venom working solution (0.5 lg/ml) used in all heart experiments was freshly prepared in Ringer solution.…”

Section: Scorpions and Venom Collectionmentioning

confidence: 99%

“…Scorpion venom is a heterogeneous mixture of substances including nucleotides, biogenic amines, lipids, peptides and proteins. Recent venomics studies revealed that each scorpion species may contain more than 150 toxins and venom peptides (Rodriguez de la Vega and Possani, 2005;Abdel-Rahman et al, 2013. Peptides with biological properties can be classified into non-disulfide-bridged peptides (NDBPs) and disulfide-bridged peptides (DBPs) (Possani et al, 1999;Zeng et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Cardiac disorders and mode of action of the Egyptian scorpion venom Androctonus bicolor on isolated toad’s heart

Abdel-Rahman

Ayed

Abdel–Mottaleb

et al. 2015

The Journal of Basic & Applied Zoology

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Scorpion venom is a complex mixture of components with various pharmacological and toxicological effects. It is characterized by the presence of a large number of toxins that specifically interact with ion channels of excitable cells. The Egyptian scorpion Androctonus bicolor belongs to the family of Buthidae and until now no information is available about the effect of its venom on cardiac muscles. Using an in vitro approach, cardiotoxicity and mode of action of A. bicolor venom on isolated toad's heart were investigated. Direct application of scorpion venom (0.5 lg/ml) into isolated toad's heart induced a remarkable bradycardia concomitant with a protraction in the conduction time (P-R interval). In the meantime, a significant increase in the R-wave amplitude (ventricular contraction) was noticed after 5 min of venom perfusion. Various cases of cardiac disorders were recorded such as sinus arrhythmias, ectopic beats and different degrees of heart block. Through using different autonomic and ion channel blockers, the possible mechanism of action of A. bicolor venom on isolated toad's heart was revealed. The application of both atropine (4 lg/ml) and verapamil (5 lg/ml) could not alleviate the pronounced negative chronotropic and positive inotropic effects. Meanwhile, a significant decrease in the R-wave amplitude was observed after propranolol (5 lg/ml) application. In conclusion, our findings indicate that the venom of A. bicolor directly influenced the cardiac electrical activity of toads through b-adrenergic receptors. The direct effect of this venom on cardiac tissues may significantly contribute in the development of several cardiotoxic effects following scorpion sting.

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“…Although La1 is the most abundant component in the venom, its biological function is still unknown. Recently, many scorpion peptides with similar sequences to La1 have been reported and are termed 'La1-like peptides' (Abdel-Rahman et al, 2013). Intriguingly, peptides homologous to La1 were found not only in scorpions, but also in ticks (Ribeiro et al, 2011), insects (Sheldon et al, 2007) and shrimps (Chen et al, 2011), suggesting that La1-like peptides have an important biological role.…”

Section: Introductionmentioning

confidence: 99%

Crystallization and preliminary X-ray diffraction studies of La1 fromLiocheles australasiae

et al. 2014

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A novel scorpion venom peptide, La1 from Liocheles australasiae, with a molecular weight of 7.8 kDa, is presumed to possess a single von Willebrand factor type C (VWC) domain, a common protein module, based on the position of eight Cys residues in its sequence. The biological function of La1 is still unknown. Deciphering its three-dimensional structure will be helpful in understanding its biological function. La1 was crystallized by the sitting-drop vapour-diffusion method using magnesium sulfate as a precipitant. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 63.0, b = 30.2, c = 32.3 Å , = 108.5, and diffracted to 1.9 Å resolution. The calculated V M based on one molecule per asymmetric unit was 1.87 Å 3 Da À1. The solvent content was 34.1%.

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Venom proteomic and venomous glands transcriptomic analysis of the Egyptian scorpion Scorpio maurus palmatus (Arachnida: Scorpionidae)

Cited by 82 publications

References 82 publications

The transcriptome recipe for the venom cocktail of Tityus bahiensis scorpion

The transcriptome recipe for the venom cocktail of Tityus bahiensis scorpion

Cardiac disorders and mode of action of the Egyptian scorpion venom Androctonus bicolor on isolated toad’s heart

Crystallization and preliminary X-ray diffraction studies of La1 fromLiocheles australasiae

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