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At least 847 records · Page 47Linked to original sources
PubMed1993

Antibodies cross-reactive with the scorpion-toxin II from Androctonus australis Hector elicited in mice by a synthetic peptide.

With the aim of developing active protection against the noxious effects provoked in humans by scorpion stings, the possibility of eliciting toxin reactive antibodies by immunization with a short peptide was assessed in mice. The amino acid sequence of residues 50 to 59 of Androctonus australis Hector toxin II was chosen, on the basis of previous results indicating that rabbit anti-(50-59) antibodies neutralize the biological effects of the parent toxin. The peptide was prepared by solid-phase synthesis procedures and used in different forms (free, linearly polymerized, coupled to KLH, coupled to a low-molecular weight B-lymphocyte activator) in order to immunize groups of non-congenic NMRI or congenic C57BL/6 mice. The reactivities of each serum with the peptide and with the toxin were assessed in ELISA. Strong reactivities with both the peptide (mean titer over 1:52,600) and the toxin (mean titer 1:800) were observed in all mice from the group that received the KLH-coupled peptide. However, mouse immune sera failed either to recognize the toxin in a liquid-phase radioimmunoassay or to neutralize the lethal effects of the toxin. The requirements, in terms of affinity and recognition of native conformation, for anti-peptide antibodies to display neutralizing properties are discussed.

Amino Acid Sequence↗
PubMed2004

Evolutionary trace analysis of scorpion toxins specific for K-channels.

Scorpion alpha-K(+) channel toxins are a large family of polypeptides with a similar structure but diverse pharmacological activities. Despite many structural and functional data available at present, little progress has been made in understanding the toxin's molecular basis responsible for the functional diversification. In this paper, we report the first complete cDNA sequences of toxins belonging to subfamily 6 and identify five new members, called alpha-KTx 6.6-6.10. By analyzing the rates of mutations that occurred in the corresponding cDNAs, we suggest that accelerated evolution in toxin-coding regions may be associated with the functional diversification of this subfamily. To pinpoint sites probably involved in the functional diversity of alpha-KTx family, we analyzed this family of sequences using the evolutionary trace method. This analysis highlighted one channel-binding surface common for all the members. This surface is composed of one conserved lysine residue at position 29 assisted by other residues at positions 10, 26, 27, 32, 34, and 36. Of them, the positions 29, 32, and 34 have been reported to be the most major determinants of channel specificity. Interestingly, another contrary surface was also observed at a higher evolutionary time cut-off value, which may be involved in the binding of ERG (ether-a-go-go-related gene) channel-specific toxins. The good match between the trace residues and the functional epitopes of the toxins suggested that the evolutionary trace results reported here can be applied to predict channel-binding sites of the toxins. Because, the side-chain variation in the trace positions is strongly linked with the functional alteration and channel-binding surface transfer of alpha-KTx family, we conclude that our findings should also be important for the rational design of new toxins targeting a given potassium channel with high selectivity.

Animals↗
PubMed2002

Determination of species-specific components in the venom of Parabuthus scorpions from southern Africa using matrix-assisted laser desorption time-of-flight mass spectrometry.

The aim of the present study was to analyze mass spectra of scorpions belonging to the genus Parabuthus (Pocock 1890) by means of matrix-assisted laser desorption time-of-flight mass spectrometry (MALDI-TOFMS) and to construct a species-specific venom code for species identification. The venom compositions of sixteen Parabuthus species, occurring in southern Africa, were characterized using representative peaks in the molecular mass range of 6400-8400 Da. This mass range is characteristic for the typical long-chain neurotoxins influencing sodium channels. Only a few of these peptides have been sequenced up to now. The impetus for development of these species-specific profiles was the observation of unique, highly reproducible mass spectral peaks within a specific species. An identification label for all the different species could be found using a minimum number of peaks. MALDI-TOFMS is therefore proposed as a complementary method to morphological and behavioural characteristics for species and ultimately subspecies discrimination.

Africa, Southern↗
PubMed1999

Solution structure of a beta-neurotoxin from the New World scorpion Centruroides sculpturatus Ewing.

We report the detailed solution structure of the 7.2 kDa protein CsE-I, a beta-neurotoxin from the New World scorpion Centruroides sculpturatus Ewing. This toxin binds to sodium channels, but unlike the alpha-neurotoxins, shifts the voltage of activation toward more negative potentials causing the membrane to fire spontaneously. Sequence-specific proton NMR assignments were made using 600 MHz 2D-NMR data. Distance geometry and dynamical simulated annealing refinements were performed using experimental distance and torsion angle constraints from NOESY and pH-COSY data. A family of 40 structures without constraint violations was generated, and an energy-minimized average structure was computed. The backbone conformation of the CsE-I toxin shows similar secondary structural features as the prototypical alpha-neurotoxin, CsE-v3, and is characterized by a short 2(1/2)-turn alpha-helix and a 3-strand antiparallel beta-sheet, both held together by disulfide bridges. The RMSD for the backbone atoms between CsE-I and CsE-v3 is 1.48 A. Despite this similarity in the overall backbone folding, the these two proteins show some important differences in the primary structure (sequence) and electrostatic potential surfaces. Our studies provide a basis for unravelling the role of these differences in relation to the known differences in the receptor sites on the voltage sensitive sodium channel for the alpha- and beta-neurotoxins.

Amino Acid Sequence↗
PubMed2000

Blockage of human T lymphocyte Kv1.3 channels by Pi1, a novel class of scorpion toxin.

Using the patch-clamp technique we determined that Pandinus imperator toxin Pi1, a recently described peptide toxin having four disulfide bridges instead of the usual three in scorpion toxins, blocked Kv1.3 channels of human T lymphocytes from the extracellular side with a 1:1 stoichiometry. Kv1.3 block was instantaneous and removable with toxin-free extracellular solution. The toxin did not influence activation or inactivation of the channels. We found that Pi1 blocked Kv1.3 with less affinity (K(d) = 11.4 nM) than the structurally related three disulfide bridge containing toxins Pi2 (50 pM) and Pi3 (0.5 nM). The fourth disulfide bridge in Pi1 had no influence on the channel binding ability of the toxin; the less effective block was due to differences in amino acid side chain properties at positions 11 and 35.

Amino Acid Sequence↗
PubMed2001

OsK2, a new selective inhibitor of Kv1.2 potassium channels purified from the venom of the scorpion Orthochirus scrobiculosus.

A novel inhibitor of voltage-gated K(+) channels has been purified to homogeneity from the venom of the black scorpion Orthochirus scrobiculosus. This toxin, named OsK2, has been characterized as a 28-residue peptide, containing six conserved cysteine residues and was shown to be a potent and selective blocker of Kv1.2 channels (K(d) = 97 nM). OsK2 is the second member of the 13th subfamily of short-chain K(+) channel-blocking peptides known thus far and is therefore called alpha-KTx 13.2.

Amino Acid Sequence↗
PubMed1996

Two novel toxins from the venom of the scorpion Pandinus imperator show that the N-terminal amino acid sequence is important for their affinities towards Shaker B K+ channels.

Two novel peptides were purified from the venom of the scorpion Pandinus imperator, and were named Pi2 and Pi3. Their complete primary structures were determined and their blocking effects on Shaker B K+ channels were studied. Both peptides contain 35 amino acids residues, compacted by three disulfide bridges, and reversibly block the Shaker B K+ channels. They have only one amino acid changed in their sequence, at position 7 (a proline for a glutamic acid). Whereas peptide Pi2, containing the Pro7, binds the Shaker B K+ channels with a Kd of 8.2 nm, peptide Pi3 containing the Glu7 residue has a much lower affinity of 140 nm. Both peptides are capable of displacing the binding of 125I-noxiustoxin to brain synaptosome membranes. Since these two novel peptides are about 50% identical to noxiustoxin, the present results support previous data published by our group showing that the amino-terminal region of noxiustoxin, and also the amino-terminal sequence of the newly purified homologues: Pi2, and Pi3, are important for the recognition of potassium channels.

Amino Acid Sequence↗
PubMed2006

In vitro leishmanicidal activity of Tityus discrepans scorpion venom.

Leishmania parasites are sensitive to peptides with antimicrobial and ion-channel inhibitory activity. Because scorpion venoms are rich sources of such peptides, the leishmanicidal effect of Tityus discrepans venom was investigated. A negative correlation between cell growth and venom concentration was observed for venom-treated cultures of Leishmania (L.) mexicana mexicana promastigotes; 50% growth inhibition was obtained at 0.4 microg/ml. Light microscopy showed rounded, highly vacuolated L. (L.) m. mexicana cells with impaired flagellar motion after 15 min of incubation at 35 microg/ml. Ultrastructural studies confirmed an intense cytoplasm vacuolation and also enlargement of the flagellar pocket. Survival rates for New World Leishmania promastigotes (75% venom effective concentration, microg/ml) obtained after acute (1 h) venom toxicity tests were: L. (L.) m. mexicana (2.3), Leishmania (V.) braziliensis (11.3), and Leishmania (L.) chagasi (56.2). Heat (90 degrees C) treatment of venom and fraction TdII abolished most of their leishmanicidal effect. Acute toxicity assays performed with Sephadex G-50 fractions indicated that leishmanicidal activity is associated with the venom lowest molecular mass components (2.8-7.4 kDa), as determined by MALDI-TOF mass spectrometry.

Animals↗
PubMed2005

Synthesis, expression and purification of a type of chlorotoxin-like peptide from the scorpion, Buthus martensii Karsch, and its acute toxicity analysis.

A gene, rBmK Cta, encoding a chlorotoxin-like peptide from the scorpion, Buthus martensii Karsch, was synthesized according to the sequence optimized for codon usage in Escherichia coli and was expressed in E. coli BL21 (DE3) using a pExSecI expression system in which the IgG-binding domain-ZZ of protein A is fused to the N-terminal of rBmK CTa. The fusion protein, ZZ-rBmK CTa, was expressed in soluble form (7.8 mg l(-1)) and was purified to give a single band on SDS-PAGE. The domain-ZZ of fusion protein ZZ-rBmK CTa was removed by cleavage of an Asn-Gly peptide bond with hydroxylamine. The rBmK CTa was separated from the IgG-binding moiety by a second passage through the IgG affinity column. Western blot analysis demonstrated that this protein was rBmK CTa. Acute toxicity assay in mice demonstrated that the rBmK CTa had an LD(50) value of 4.3 mg kg(-1).

Animals↗
PubMed2006

Polyclonal antibody against a recombinant chlorotoxin-like peptide from the Chinese scorpion and detection of its putative receptors in human glioma cells.

The nucleotide sequence of a type of chlorotoxin-like peptide, an inhibitor of small-conductance Cl(-) channels, from the scorpion, Buthus martensii Karsch, was synthesized (named rBmK CTa) according to the sequence optimized for codon usage in E. coli. It was over-expressed using a pExSecI expression system and purified to homogeneity. Polycolonal antibodies to the purified protein were raised in rats. Overlay assay and pull-down assay showed that this toxin specially binds to two proteins in the glioma cells with corresponding molecular weights of about 80 and 35 kDa. They may serve as candidate receptors or alternative cellular component for interaction with rBmK CTa.

Animals↗
PubMed1980

Potential-dependent interaction of toxin from venom of the scorpion Buthus eupeus with sodium channels in myelinated fibre: voltage clamp experiments.

1. The steady-state characteristics of the sodium channel gating in the nodal membrane were determined under voltage clamp conditions before and after treatment with toxins from the venom of scorpion, Buthus eupeus. 2. The apparent binding constant (KA) of the toxin was determined for different levels of the membrane potential. At potentials more negative than -120 mV, KA tends to a constant level. KA is maximum at about -80 mV, and it decreases as the potential is teduced to 0 mV. 3. A model assuming that the voltage dependency of KA is mainly due to the difference in electrical energy between inactivated states of normal and poisoned channels is proposed. An additional decrease in overall binding of toxin results from the transition of a fraction of the sodium channels into the state of slow inactivation.

Animals↗
PubMed1986

Identification of two toxins from scorpion (Leiurus quinquestriatus) venom which block distinct classes of calcium-activated potassium channel.

Two polypeptide toxins from scorpion (Leiurus quinquestriatus) venom which block distinct classes of calcium-activated potassium channels have been identified and partially purified. One toxin, at 50-100 ng/ml, blocks apamin-sensitive potassium fluxes in hepatocytes and inhibits [125I]monoiodoapamin binding. The other, more basic, toxin blocks apamin-insensitive potassium fluxes in erythrocytes at 200 ng/ml and, to our knowledge, is the first toxin shown to block the erythrocyte calcium-activated potassium channel with high affinity. The possible co-identity of this latter toxin with charybdotoxin is discussed.

Animals↗
PubMed1993

The genomic region encoding toxin gamma from the scorpion Tityus serrulatus contains an intron.

The gene encoding toxin gamma from the scorpion, Tityus serrulatus, was amplified by PCR from genomic DNA employing synthetic oligonucleotides designed from the reported cDNA sequence. The nucleotide sequence of this gene reveals the presence of an intron of 475 base pairs (bp) which interrupts the region that encodes the signal peptide of the precursor toxin. A comparison of the intron boundary sequences of the gamma toxin gene with ones from other arachnid genes is also presented.

Animals↗
PubMed1993

Primary structure determination and cloning of the cDNA encoding toxin 4 of the scorpion Centruroides noxius Hoffmann.

A peptide (toxin II-10), shown to be a Na+ channel blocker, was purified from the venom of the scorpion Centruroides noxius Hoffmann and sequenced by Edman degradation. It has 66 amino acid residues with the C-terminal residue (asparagine) amidated, as demonstrated by mass spectrometry. In addition, we report the cloning and the nucleotide sequence of the cDNA (CngtV) that codes for this toxin. We discuss the mechanism for processing the precursor peptide to its final form and compare the primary structure to that of other Na+ channel toxins. Two distinct groups of toxins seem to emerge from this comparison, suggesting a structure-function relationship of these peptides towards the recognition of either mammalian or insect tissues.

Amino Acid Sequence↗
PubMed1994

The disulfide bridges of toxin 2 from the scorpion Centruroides noxius Hoffmann and its three-dimensional structure calculated using the coordinates of variant 3 from Centruroides sculpturatus.

The disulfide bridges of toxin 2 from the venom of the scorpion Centruroides noxius Hoffmann were found by amino acid sequence determination of fragments of native toxin, produced by enzymatic cleavage and separated by high-performance liquid chromatography (HPLC). They are: Cys12-Cys65, Cys16-Cys41, Cys25-Cys46 and Cys29-Cys48. The coordinates of the X-ray diffraction structure of toxin variant 3 of C. sculpturatus [(1980) Proc. Natl. Acad. Sci. USA 77, 6496-6500] were used to construct a three-dimensional model of toxin 2. All the amino acid replacements were easily accommodated, and the modeled structure reveals a clustered pattern of sequence variation, which may help to identify residues responsible for functional differences among toxins of mammals and insects.

Amino Acid Sequence↗
PubMed1994

Biochemical, pharmacological and genomic characterisation of Ts IV, an alpha-toxin from the venom of the South American scorpion Tityus serrulatus.

The venom of the scorpion, Tityus serrulatus, was fractionated to investigate the chemical and pharmacological properties of its alpha-toxin content. Three alpha-toxins (Ts III, Ts IV and Ts V) were purified by conventional chromatography (gel filtration and ion-exchange chromatography), followed by immunoaffinity chromatography. Competition experiments using reference alpha- and beta-toxins suggested that these alpha-toxins were contaminated with around 0.01% of beta-toxin. The sequence of the first 30 amino acids of Ts IV was established. Using an oligonucleotide probe, a cDNA encoding its precursor was cloned from a venom gland cDNA library. The primary structure deduced from the cDNA nucleotide sequence provides possible explanations for the polymorphism of these three molecules.

Amino Acid Sequence↗
PubMed1990

Crystallization and preliminary X-ray study of AaH IT2, and insect-specific toxin from the scorpion Androctonus australis Hector.

An insect-specific toxin from the venom of the scorpion Androctonus australis Hector has been crystallized. The crystals are orthorhombic, space groups P2(1)2(1)2(1), with cell dimensions a = 66.4 A, b = 52.5 A and c = 36.1 A. Calculations based on the unit cell volume and toxin molecular mass suggest that there are two molecules in the asymmetric unit.

Animals↗
PubMed1992

Issues in management of scorpion sting in children.

All children admitted to Madina Maternity and Children's Hospital, Saudi Arabia, in 1989 because of scorpion stings (primarily Leiurus quinquestriatus) were studied. Of 96 children studied, 20 suffered either shock, pulmonary oedema or both. These 20 shared characteristic clinical features such as vomiting, priapism and failure to maintain normal temperature and/or blood pressure. The management protocol emphasized fluid restriction and the i.v. administration of venom antitoxin. Doubling the recommended dose did not improve the outcome. Two children died and the rest recovered.

Adolescent↗