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Screening of the venoms of two Parabuthus scorpion species on isolated cardiomyocytes.

Crude, diluted venoms of Parabuthus transvaalicus and P. granulatus were tested on isolated cardiomyocytes. Ventricular myocytes were subjected to hypercontractility tests and whole-cell voltage clamp. Both venoms had a profound influence on the hypercontractility of cardiomyocytes, which was markedly decreased when they were pre-absorbed with commercial antiserum. Whole-cell clamp results showed an increase in the sodium current, and a retardation of the time course of inactivation, implicating the presence of an alpha toxin in both venoms.

Animals↗

Solution structure of BmKTX, a K+ blocker toxin from the Chinese scorpion Buthus Martensi.

BmKTX is a toxin recently purified from the venom of Buthus Martensi, which belongs to the kaliotoxin family. We have determined its solution structure by use of conventional two-dimensional NMR techniques followed by distance-geometry and energy minimization. The calculated structure is composed of a short alpha-helix (residues 14 to 20) connected by a tight turn to a two-stranded antiparallel beta-sheet (sequences 25-27 and 32-34). The beta-turn connecting these strands belongs to type I. The N-terminal segment (sequence 1 to 8) runs parallel to the beta-sheet although it cannot be considered as a third strand. Comparison of the conformation of BmKTX and toxins of the kaliotoxin family clearly demonstrates that they are highly related. Therefore, analysis of the residues belonging to the interacting surface of those toxins allows us to propose a functional map of BmKTX slightly different from the one of KTX and AgTX2, which may explain the variations in affinities of these toxins towards the Kv1.3 channels.

Amino Acid Sequence↗

The Androctonus australis garzoni scorpion venom contains toxins that selectively affect voltage-dependent K(+)-channels in cerebellum granular cells.

A purified peptide from Androctonus australis Garzoni venom (AaG) affects selectively a K(+)-current recorded from cerebellum granular cells. This current is characterized by fast activating and inactivating kinetics similar to an IA-type current. Addition of 2 microM peptide Aa1 (from Androctonus australis, toxin 1) to the external side of the channel suppressed completely and in a selective manner the IA-type current, with an IC50 value of 130 nM, whereas in the same conditions, the other potassium current, identified as delayed rectifier (Id), was not affected. Additionally, we show that another partially purified peptide (III-12) from the same venom was able to block reversibly both K(+)-currents.

Animals↗

Characterization of a new peptide from Tityus serrulatus scorpion venom which is a ligand of the apamin-binding site.

A new ligand (Ts kappa) of the apamin binding site on rat brain synaptosomes (K0.5 = 300 pM) was purified and characterized from the venom of Tityus serrulatus. It is a polypeptide toxin of 35 amino acid residues, with three disulfide bridges. Its cDNA was amplified from a venom gland cDNA library and the nucleotide sequence determined. A model of Ts kappa was constructed by amino acid replacement using charybdotoxin structure as determined by 1H nuclear magnetic resonance as starting model.

Amino Acid Sequence↗

Scorpion sting.

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Adult↗