Venom Of Androctonus Australis Research Articles

Comparative analyses and implications for antivenom serotherapy of four Moroccan scorpion Buthus occitanus venoms: Subspecies tunetanus, paris, malhommei, and mardochei

Temporary passive immunity such as serotherapy against venoms requires the full knowledge of all venom's components. Here, four venoms from Moroccan common yellow scorpions belonging to Buthus occitanus, subspecies tunetanus, paris, malhommei, and mardochei, all collected in four different restricted areas, were analysed in deep. They were fractionated by reversed-phase high-performance liquid chromatography (RP-HPLC) and their molecular masse profile determined by off-line MALDI-TOF mass spectrometry. Characterisation of their main components was achieved by enzyme-linked immunosorbent assay (ELISA) using specific antisera against the major lethal scorpion toxins identified so far, i.e. voltage-gated sodium channels (Nav) modulators α- and β-toxins, as well as diverse potassium channel pore blocker toxins. For fractions with identical RP-HPLC retention times, we observe that their relative quantities show large differences. Moreover, identical masses present simultaneously in the four venoms are infrequent. ELISAs show that the majority of the RP-HPLC compounds cross-react with the antiserum against the “α-like” toxin Bot I, which has been previously identified in the Algerian Buthus occitanus tunetanus venom. Moreover, minor fractions were recognised by the antiserum against the highly lethal “classical” α-toxin of reference AaH II from the Androctonus australis venom. As such, our results bring new sights for further improving scorpion venom serotherapy in Morocco.

34. Androctonus australis venom induces lung injury by dependent mechanisms on mast cells activation

34. Androctonus australis venom induces lung injury by dependent mechanisms on mast cells activation

New analysis of the toxic compounds from the Androctonus mauretanicus mauretanicus scorpion venom

Scorpion venoms are very complex mixtures of molecules, most of which are peptides displaying different kinds of biological activity. Indeed, these peptides specifically bind to a variety of pharmacological targets, in particular ionic channels located in prey tissues, resulting in neurotoxic effects. Toxins modulating Na +, K +, Ca 2+ and Cl − currents have been described in scorpion venoms. In this work, we have used several specific antibodies raised against the most lethal scorpion toxins already described to screen the Moroccan scorpion Androctonus mauretanicus mauretanicus venom in order to characterize new compounds. This immunological screening was also implemented by toxicity tests in mice and with mass spectrometry study, providing new informations on the molecular composition of this venom. In fine, we were able to determine the molecular masses of 70–80 different compounds. According to the immunological data obtained, many toxins cross-react with three sera raised against the most lethal α-toxins found in North African scorpion venoms, but not at all with those raised against the main β-toxins from South and North American venoms. Some of the previously described toxins from Androctonus mauretanicus mauretanicus venom could thus be detected by combining immunological tests, toxicity in mice and molecular masses. Among these toxins, one of them, which showed a mild cross-reaction with the serum raised against AaH I (a highly potent toxin from the venom of Androctonus australis), was identified as Amm III and fully sequenced.

Novel structural class of four disulfide-bridged peptides from Tityus serrulatus venom

A new structural class of short peptides folded by four disulfide-bridges was found in the venom of the Brazilian scorpion Tityus serrulatus. Peptides were put on evidence independently by means of two different approaches of structurally guided prospection. First, a cDNA sequence was obtained using a degenerate primer constructed according to the C-terminal sequence of kaliotoxin (KTx 2), from the Androctonus australis venom. Second, MALDI-TOF mass spectrometry analyses of toxic fraction FIII from T. serrulatus venom revealed a family of molecules ranging approximately from 2900 to 3000 Da. Three new peptides were isolated and named TsPep1, TsPep2, and TsPep3. Biochemical characterization showed that they are 29 amino acids long, constrained by a new pattern of four disulfide-bridges. These results enable us to classify these new molecules as part of a novel structural class of short peptides from scorpion venoms.

The role of nitric oxide on the relaxations of rabbit corpus cavernosum induced by Androctonus australis and Buthotus judaicus scorpion venoms

In this study, we have investigated the relaxing effects of both Androctonus australis venom (AAV) and Buthotus judaicus venom (BJV) on the rabbit corpus cavernosum (RbCC) smooth muscle strips. The RbCC strips were mounted in a cascade system and superfused with warmed and gassed Krebs solution. The nitric oxide (NO) synthesis inhibitor Nω-nitro-l-arginine methyl ester (l-NAME, 10μM), but not d-NAME (10μM), significantly inhibited the RbCC relaxations induced by acetylcholine (ACh, 0.6nmol), AAV (30μg) and BJV (30μg). Subsequent infusion of l-arginine (300μM), but not of d-arginine (300μM), partially restored the relaxations evoked by these agents. The brain NO synthase inhibitor 7-nitroindazole (7-NI, 10μM) also inhibited the relaxant responses elicited by the scorpion venoms. The guanylyl cyclase inhibitors methylene blue (MB, 30μM) and 1H-[1,2,4] oxadiazolo [4,3,-alquinoxalin-1-one] (ODQ, 10μM) virtually abolished the relaxations induced by either AAV or BJV. The infusion of muscarinic receptor antagonists such as scopolamine and atropine (1μM, each) completely abolished the ACh-induced relaxations but had no effect on those evoked by the scorpion venoms. The Na+ channel blocker tetrodotoxin (1μM) prevented the relaxations evoked by both AAV and BJV. Thus, NO released from nitrergic nerve fibres mediates the relaxations elicited by AAV and BJV in the rabbit cavernosal tissue.

Rapid purification and molecular modeling of AaIT peptides from venom of Androctonus australis

As recombinant viruses expressing scorpion toxins are moving closer toward the market, it is important to obtain large amounts of pure toxin for biochemical characterization and the evaluation of biological activity in nontarget organisms. In the past, we purified a large amount of Androctonus australis anti-insect toxin (AaIT) present in the venom of A. australis with an analytical reversed-phase column by repeated runs of crude sample. We now report 20 times improved efficiency and speed of the purification by employing a preparative reversed-phase column. In just two consecutive HPLC steps, almost 1 mg of AaIT was obtained from 70 mg crude venom. Furthermore, additional AaIT was obtained from side fractions in a second HPLC run. Recently discovered insect selective toxin, AaIT5, was isolated simultaneously from the same venom batch. It shows different biological toxicity symptoms than the known excitatory and depressant insect toxins. AaIT5 gave 100% mortality with a dose of less than 1.3 μg against fourth-instar tobacco budworms Heliothis virescens 24 h after injection. During the purification process, we implemented mass spectrometry in addition to bioassays to monitor the presence of AaIT and AaIT5 in the HPLC fractions. Mass spectrometric screening can unambiguously follow the purification process and can greatly facilitate and expedite the downstream purification of AaIT and AaIT5 eliminating the number of bioassays required. Further, electrospray ionization was compared with matrix-assisted desorption/ionization and evaluated as a method of choice for mass spectrometric characterization of fractions from the venom purification for it provided higher mass accuracy and relative quantitation capability. Molecular models were built for AaIT5, excitatory toxin AaIT4, and depressant toxin LqhIT2. Three-dimensional structure of AaIT5 was compared with structures of the other two toxins, suggesting that AaIT5 is similar to depressant toxins. Arch. Insect Biochem. Physiol. 38:53–65, 1998. © 1998 Wiley-Liss, Inc.

The kaliotoxin family enlarged. Purification, characterization, and precursor nucleotide sequence of KTX2 from Androctonus australis venom

Kaliotoxin (KTX) has been originally described as an inhibitor of the intermediate conductance Ca(2+)-activated K+ channel (Crest, M., Jacquet, G., Gola, M., Zerrouk, H., Benslimane, A., Rochat, H., Mansuelle, P., and Martin-Eauclaire, M.-F. (1992) J. Biol. Chem. 267, 1640-1647). However, the radioiodinated 125I-KTX-(1-37) was also able to bind to the dendrotoxin sensitive voltage-dependent K+ channel (Romi, R., Crest, M., Gola, M., Sampieri, F., Jacquet, G., Zerrouk, H., Mansuelle, P., Sorokine, O., Van Dorsselaer, A., Rochat, H., Martin-Eauclaire, M.-F., and Van Rietschoten, J. (1993) J. Biol. Chem. 268, 26302-26309). By following the ability to compete with 125I-KTX-(1-37) for binding to its receptor on rat brain synaptosomes, a new kaliotoxin-like peptide, KTX2, was isolated from Androctonus australis scorpion venom. It is a 37-amino acid residue peptide, and its sequence shares 76% identity with KTX. The differences between the two peptides concern the NH2-terminal region and the residues 31 and 34 located in the region involved in the channel recognition. These differences may explain the 5-fold decrease of the molluscan Ca(2+)-activated K+ channel blockage by KTX2 (kd = 135 nM) as well as of its binding affinity to rat brain synaptosomes (IC50 = 50 pM), compared with KTX. Specific antibodies raised against KTX-(1-37) were not able to recognize KTX2. Using degenerate primers, a 370-base pair cDNA encoding the KTX2 precursor was amplified by polymerase chain reaction from a cDNA library of A. australis venom glands. It encoded a presumed signal peptide of 22 residues followed by the sequence of the mature peptide.

Effects of a scorpion toxin from Androctonus australis venom on action potential of neuroblastoma cells in culture

Summary The effect of toxin II from the venom of Androctonus australis on the action potential of clone NIE-115 of mouse neuroblastoma cells was studied. The toxin increased quasi-irreversibly duration and amplitude of spike and its time derivative; half-maximum effects were obtained at 2.5, 0.3 and 0.4 nM, respectively. Toxin action was potentiated by veratridine and inhibited by tetrodotoxin. Washing suppressed the effect of veratridine and tetrodotoxin but was ineffective on scorpion toxin effect. As in nerve axons and neuromuscular preparations, the studied toxin affects the closing of the Na + channel and likely the opening of the K + channel.

Effects of scorpion venom on squid axon membranes.

Effects of scorpion venom on squid axon membranes.

Effect of Drugs on Survival Time from Scorpion: Envenomation

Androctonus australis venom at various dilutions was administered to matched groups of mice and the effects on survival time and number determined for various classes of therapeutic agents. Meperidine and other narcotics were consistently deleterious to envenomed animals as were alcohol and calcium acetylsalicylate carbamide. Neither corticosteroids nor muscle relaxants were beneficial. With tran-quilizing agents, meprobamate tended to increase survival time, while reserpine markedly curtailed survival.