Purification and characterization of a β‐toxin from the venom of the African scorpion <i>Leiurus quinquestriatus</i>

Rack, Michael; Richter, D.; Rubly, N.

doi:10.1016/0014-5793(87)80034-0

Cited by 11 publications

(4 citation statements)

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“…Yet, scorpion polypeptides that resemble ‘New World’β‐toxins have been reported in the ‘Old World’ and include the nontoxic polypeptide, AahSTR1 [38], the glycosylated toxin, Aah6 [39], and the anti‐insect selective excitatory and depressant toxin groups [2,12,17,20]. In addition, polypeptides with some β‐toxin properties have been found in the venom of the old world scorpions, Leiurus quinquestriatus hebraeus [40] and Buthus martensii Karsch [25]. Another peculiar toxin that competes for both α and β‐toxin receptor sites in rat brain synaptosomes, AahIT4, seems to be related to β‐toxins because it was recognized by antibodies raised against the β‐toxin, Css2, but not by antibodies against the α‐toxin, Aah2, or the excitatory toxin, AahIT [23].…”

Section: Discussionmentioning

confidence: 99%

An ‘Old World’ scorpion β‐toxin that recognizes both insect and mammalian sodium channels

Gordon

Ilan

Zilberberg

et al. 2003

European Journal of Biochemistry

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Scorpion toxins that affect sodium channel (NaCh) gating in excitable cells are divided into a-and b-classes. Whereas a-toxins have been found in scorpions throughout the world, anti-mammalian b-toxins have been assigned, thus far, to ÔNew WorldÕ scorpions while anti-insect selective b-toxins (depressant and excitatory) have been described only in the ÔOld WorldÕ. 2This distribution suggested that diversification of b-toxins into distinct pharmacological groups occurred after the separation of the continents, 150 million years ago. We have characterized a unique toxin, Lqhb1, from the ÔOld WorldÕ scorpion, Leiurus quinquestriatus hebraeus, that resembles in sequence and activity both ÔNew WorldÕ b-toxins as well as ÔOld WorldÕ depressant toxins. Lqhb1 competes, with apparent high affinity, with anti-insect and anti-mammalian b-toxins for binding to cockroach and rat brain synaptosomes, respectively. Surprisingly, Lqhb1 also competes with an anti-mammalian a-toxin on binding to rat brain NaChs. Analysis of Lqhb1 effects on rat brain and Drosophila Para NaChs expressed in Xenopus oocytes revealed a shift in the voltage-dependence of activation to more negative membrane potentials and a reduction in sodium peak currents in a manner typifying b-toxin activity. Moreover, Lqhb1 resembles b-toxins by having a weak effect on cardiac NaChs and a marked effect on rat brain and skeletal muscle NaChs 3. These multifaceted features suggest that Lqhb1 may represent an ancestral b-toxin group in ÔOld WorldÕ scorpions that gave rise, after the separation of the continents, to depressant toxins in ÔOld WorldÕ scorpions and to various b-toxin subgroups in ÔNew WorldÕ scorpions.Keywords: scorpion toxins; sodium channel subtypes; toxin diversification.Scorpion Ôlong chainÕ toxins affecting voltage-gated sodium channels (NaCh) are polypeptides of 61-76 amino acids long that traditionally are divided between two major classes, a and b, according to their physiological effects on channel gating and their binding properties [1][2][3]. a-Toxins slow sodium channel inactivation upon binding to a homologous cluster of binding sites named receptor site-3, and are subdivided into distinct groups according to their potency for mammalian and insect receptors and their affinity for sodium channel subtypes [2,[4][5][6][7]. a-Toxins predominate in the venom of Buthidae scorpions of the ÔOld WorldÕ (Africa and Asia), but some representatives have been also identified in ÔNew WorldÕ (America) scorpions [1]. b-Toxins shift the activation voltage of sodium channels to more negative membrane potentials upon binding to receptor site-4 [2,7,8], and vary greatly in their effects on various animals. Css2 and Css4 (from Centruroides suffusus suffusus) show specificity for mammals [1]; Cll1 (from C. limpidus limpidus), Cn5, and Cn11 (from C. noxius) are highly effective on crustaceans [9-12]; Ts7 and Tst1 (from Tityus serrulatus and T. stigmurus), and Tbs1 and Tbs2 (from T. bahiensis) are highly effective on both insects and mammals [1,[12][13][14][15][16]...

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Section: Discussionmentioning

confidence: 99%

An ‘Old World’ scorpion β‐toxin that recognizes both insect and mammalian sodium channels

Gordon

Ilan

Zilberberg

et al. 2003

European Journal of Biochemistry

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“…The o~-scorpion and sea anemone polypeptide toxins share a common site of action (Catterall & Beress, 1978), but the scorpion toxins are about an order of magnitude more potent than the sea anemone toxins (Catterall, 1977a,b;Catterall & Beress, 1978;Krueger & Blaustein, 1980). Some scorpion venoms also contain /~-polypeptide toxins, which act at a different site than the o~-toxins (Rack, Richter & Rubly, 1987) and primarily affect channel activation rather than inactivation (Meves et al, 1986).…”

Section: Introductionmentioning

confidence: 96%

Polypeptide neurotoxins modify gating and apparent single-channel conductance of veratridine-activated sodium channels in planar lipid bilayers

Corbett

Krueger

1989

J. Membrain Biol.

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The effects of scorpion and sea anemone polypeptide toxins on partially purified veratridine (VER)-activated Na channels from rat brain were studied at the single-channel level in planar lipid bilayers. The probability of the VER-activated channel being open (Po) increased with depolarization; Po was 0.5 at -40 to -50 mV. Saxitoxin (STX) blocked VER-activated channels with an apparent dissociation constant of about 1 nM at -45 mV. The apparent single-channel conductance was approximately 9 pS, similar to that seen in VER-activated Na channels from skeletal muscle transverse tubules. Addition of sea anemone or scorpion polypeptide toxins to VER-activated Na channels resulted in a 19% increase in apparent single-channel conductance and a hyperpolarizing shift in the Po vs. Vm relation such that the channels were more likely to be open at potentials less than 40 mV. These effects of the polypeptide toxins on the single-channel properties of VER-activated Na channels may account for the previously described potentiation of VER action by polypeptide toxins.

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“…The fractionation and purification of different components of scorpion venom are mainly performed by chromatographic methods [21]. Moreover, the peculiar species-specific chromatographic profiles of venoms may also be used as an auxiliary tool in the taxonomy of scorpions [22][23][24][25][26]. In this study, we present the chromatographic profiles of three dreaded scorpion species from Saudi Arabia.…”

Section: Introductionmentioning

confidence: 99%

Rapid profiling of crude scorpion venom using liquid chromatography and its relevance to species identification

Asmari

Khan

Manthiri

2012

Acta Chromatographica

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Summary. We present the comprehensive chromatographic profiles of three scorpion species, Androctonus crassicauda, Androctonus bicolor, and Leiurus quinquestriatus, commonly inhabited to Middle East regions. Their venoms were milked by electrical stimulation, diluted with distilled water, properly mixed and centrifuged to separate the mucus from venom. The clear supernatant was filtered and the protein concentration was determined. Pre-diluted venoms were chromatographed on FPLC (fast protein liquid chromatography) and RP-HPLC (reversed-phase high-performance liquid chromatography) and the fractions were collected for molecular weight determination. Both techniques have resulted clearly distinguishable chromatographic patterns that can be used for identification of scorpion species and having a quick indication of venom toxicity.

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Purification and characterization of a β‐toxin from the venom of the African scorpion Leiurus quinquestriatus

Cited by 11 publications

References 12 publications

An ‘Old World’ scorpion β‐toxin that recognizes both insect and mammalian sodium channels

An ‘Old World’ scorpion β‐toxin that recognizes both insect and mammalian sodium channels

Polypeptide neurotoxins modify gating and apparent single-channel conductance of veratridine-activated sodium channels in planar lipid bilayers

Rapid profiling of crude scorpion venom using liquid chromatography and its relevance to species identification

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