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PubMed1999

Serum levels of cytokines in patients envenomed by Tityus serrulatus scorpion sting.

Seventeen patients stung by Tityus serrulatus scorpion were classified as mild (pain at the site of the sting, n = 6), moderate (local pain and one of the following manifestations: vomiting, psychomotor agitation, prostration, sweating, tachypnea, tachycardia and mild arterial hypertension, n = 10) and severe cases (equal moderate cases plus cardiac failure, pulmonary edema and shock, n = 1). Venous blood was sampled for biochemical and hematological analysis and for IL-1alpha, IL-6, IL-10, TNF-alpha, IFN-gamma and GM-CSF ELISAs at the time of hospital admission, 6 h (moderate and severe cases), and 12, 18, 36 and 72 h (severe case) later. Ten age-matched healthy volunteers were used as control. Increased serum levels of IL-1alpha was noticed in all patients, high levels of IL-6, IFN-gamma and GM-CSF were observed only in a patient with severe envenomation. Our data suggest that a systemic inflammatory response-like syndrome is triggered during severe envenomation caused by T. serrulatus sting and that release of cytokines may be involved in this response.

Blood Cell Count↗
PubMed1998

Behavioral, electroencephalographic, and histopathologic effects of a neuropeptide isolated from Tityus serrulatus scorpion venom in rats.

The effects of intrahippocampal administration of a neuropeptide (TS-8F toxin) isolated from Tityus serrulatus scorpion venom have been determined on behavior, limbic seizures, and neuronal degeneration in rats. Behavioral observation showed orofacial automatism, wet dog shakes, and myoclonus. Concomitantly, the electroencephalographic record showed high-frequency and high-voltage spikes that evolved to seizure activity in the hippocampus and cortex. Seven days after TS-8F toxin microinjection, neuronal damage was observed in CA1 and CA2 pyramidal cells and in granular cells of the dentate gyrus. The results suggest that TS-8F toxin may be responsible, at least in part, by the epileptic effects observed with the crude venom. Thus, this toxin may be a useful tool in the study of some neurobiological process.

Amino Acid Sequence↗
PubMed1982

The specificity of Centruroides sculpturatus Ewing (Arizona lethal scorpion) hemolymph agglutinins.

C. sculpturatus sera agglutinate human erythrocytes independently of the ABO blood group, enzyme treatment, incubation temperature or sex of the scorpions. Tested with human lymphocytes and reptile and bird erythrocytes, C. sculpturatus serum reacts like an anti-sialic acid agglutinin. With leukemic lymphocytes, titers are higher than with normal lymphocytes. Mammalian erythrocytes show characteristic agglutination patterns for C. sculpturatus for Limulus polyphemus (horseshoe crab) that suggest different receptors for agglutinins of both species. Cross absorption and elution experiments indicate the presence of at least two specific agglutinins in C. sculpturatus serum. Agglutination is inhibited by N-acetylneuraminic acid and N-glycolyneuraminic acid, for all erythrocytes tested. Calcium is required for optimal activity of C. sculpturatus agglutinins. C. sculpturatus agglutinating activity is destroyed at 65% degrees C for 20 minutes. Titers are decreased by 2-mercaptoethanol, and more so after alkylation with iodoacetic acid suggesting that disulfide bonds are present in C. sculpturatus agglutinin molecules.

ABO Blood-Group System↗
PubMedDate not supplied

Isolation and structure-functional characterization of phage display library-derived mimotopes of noxiustoxin, a neurotoxin of the scorpion Centruroides noxius Hoffmann.

Noxiustoxin (NTX) is a short-chain toxin from the venom of the scorpion Centruroides noxius Hoffmann, whose molecular structure and physiological effects have been characterized in detail, whereas the antigenic properties of this and other K(+) channel-blocking toxins are poorly studied. A monoclonal antibody against NTX, BNTX18, able to inhibit the binding of NTX to rat brain synaptosomes, was used in the present study for selecting immunoreactive peptides, mimotopes, from a 12mer and a 7mer phage library. The peptides were characterized immunologically and used for mapping the epitope on NTX. In total, 75 phage clones carrying 43 different peptides were analyzed of which 42 clones carrying 17 different peptides, twelve 12mer and five 7mer peptides, presented a single consensus motif: Leu(Ile, Val)-Tyr(Phe, Trp, Leu)-Gly-Met(Ala). All but three of the peptides containing this motif were reactive with selected mAb BNTX18 in a dot-blot assay of which eight were clearly positive in ELISA and exhibited in competition-inhibition assay the antibody binding specificity of the NTX epitope recognized by BNTX18. The two most reactive mimotopes injected into mice showed the ability to induce antibodies reacting with NTX, thus, to mimic the epitope of NTX antigenically. Sequence comparison and the analysis of the three-dimensional structure of NTX led to the proposal that residues Glu19-Leu20-Tyr21-Gly22 and the hydrophobic part of the side chain of Lys18 form the C-terminal part of the epitope. Due to the frequent presence of residues Pro, Leu, Thr, Arg, and Gln in the N-terminal part of the mimotopes, corresponding homologous residues in the N-terminal proximity of the partial epitope may be part of an additional more hydrophilic epitope element.

Amino Acid Sequence↗
PubMed2002

Molecular basis for the cross-reactivity of antibodies elicited by a natural anatoxin with alpha- and beta-toxins from the venom of Tityus serrulatus scorpion.

A non-toxic protein (TsNTxP) isolated from the venom of the noxious scorpion Tityus serrulatus (Ts) induces polyclonal antibodies cross-reactive with several toxins from the venom, in sharp contrast to anti-toxin antibodies which are toxin specific. To try to uncover the molecular basis for these unusual properties, peptide scanning experiments were performed and indicated that the N- and C-terminal parts of TsNTxP enclose continuous epitopes (residues 1-15 and 47-61). Antibodies raised against peptides corresponding to these two regions were found to have neutralizing properties against a mixture of all toxic proteins from the T. serrulatus venom, indicating that residues 1-15 and 47-61 correspond to neutralizing epitopes. The identification of key antigenic residues within these two epitopes revealed that several of them are well conserved in the amino-acid sequences of the three main toxins (Ts II, Ts IV and Ts VII) from the venom: Glu 3, Tyr 5, Asp 8, Asp 50, Trp 55 and Lys 61. A single key-residue (Glu 58) is unique to TsNTxP. By using homology modeling, a model of the three-dimensional structure of TsNTxP was obtained. The antigenically important residues from TsNTxP were found to be surface exposed, with five of them clustered on the facet of the protein reported to enclose the active site of toxins. Residues equivalent to the seven key-residues of the anatoxin were also found to be exposed in the active toxins from T. serrulatus venom. These results show that antibodies elicited by the non-toxic protein TsNTxP recognized, within the N- and C-terminal parts of toxins of T. serrulatus, conserved and surface exposed residues which might also be involved in the toxic action of the proteins.

Amino Acid Sequence↗
PubMed1999

A unified nomenclature for short-chain peptides isolated from scorpion venoms: alpha-KTx molecular subfamilies.

Peptidyl toxins are used extensively to determine the pharmacology of ion channels. Four families of peptides have been purified from scorpion venom. In this article, the classification of K+-channel-blocking peptides belonging to family 2 peptides and comprising 30-40 amino acids linked by three or four disulfide bridges, will be discussed. Evidence is provided for the existence of 12 molecular subfamilies, named alpha-KTx1-12, containing 49 different peptides. Because of the pharmacological divergence of these peptides, the principle of classification was based on a primary sequence alignment, combined with maximum parsimony and Neighbour-Joining analysis.

Amino Acid Sequence↗
PubMed2000

The binding of BmK IT2, a depressant insect-selective scorpion toxin on mammal and insect sodium channels.

Binding assay of (125)I-BmK IT2, a depressant insect-selective scorpion toxin showed two non-interacting binding sites on insect neuronal membranes: a high affinity (K(d(1))=0.65+/-0.20 nM) and low capacity (B(max(1))=0.46+/-0.13 pmol/mg protein) binding site, as well as a low-affinity (K(d(2))=78.7+/-16.4 nM) and high capacity (B(max(2))=33.1+/-8.5 pmol/mg protein) binding site. BmK IT2 could associate with and dissociate from its binding sites on insect neuronal membranes in quick manner (k(1)=5.4 x 10(5) S(-1) M(-1) and k(2)=3.2 x 10(4) S(-1) M(-1); k(-1)=7.4 x 10(-4) S(-1) and k(-2)=5.3 x 10(-3) S(-1)). The binding of (125)I-BmK IT2 to insect synaptosomes could be significantly inhibited by native BmK IT2, BmK AS and BmK AS-1 in a dose-dependent manner, and partially by BmK I, but not modified by depolarization of membrane potential and veratridine, In addition, specific binding of (125)I-BmK IT2 seem to be undetectable on rat brain synaptosomes even at high concentration. Whole cell patch-clamping recording found that BmK IT2 could partially inhibit total sodium currents of rat DRG neurons, the inhibitory effects were reversible. The results suggest that the receptor binding site of BmK IT2 on insect sodium channels might be similar to that on sodium channels of mammal peripheral nervous system, but different from that of mammal central nervous system.

Animals↗
PubMed2002

c-Fos expression in rat spinal cord induced by scorpion BmK venom via plantar subcutaneous injection.

The aim of this study was to assess the cell-type and distribution of highly activated neurons in rat spinal cord underlying nociceptive responses induced by scorpion BmK venom using Fos immunohistochemistry. BmK venom was intraplantarly injected into one hind paw of a conscious rat. Fos-like immunoreactive neurons were found to predominantly distribute at L4-5 segments in the rat spinal cord after BmK venom application. c-Fos labeling was most dense in the medial half portion of laminae I-II, moderately dense in laminae V-VI and less dense in laminae III-IV, VII-X. c-Fos labeling could be detected at 0.5 h, reached the peak at 2 h, decreased steeply from 4 h and then almost disappeared at 24 h. Ten to fifty micrograms of BmK venom was deemed to be a sufficient dosage to evoke c-Fos expression. On the other hand, c-Fos expression induced by BmK venom could be suppressed partially by systemic morphine in a dose-dependent manner. The results suggest that the different extent of activities of neuronal subpopulation in the spinal cord involved in nociceptive transmission manifesting as c-Fos expression, were mainly correlated with mechanisms underlying the generation, maintenance and/or modulation of spontaneous pain and hyperalgesia evoked by BmK venom.

Afferent Pathways↗
PubMed2000

Step-wise formation of helical structure and side-chain packing in a peptide from scorpion neurotoxin support hierarchic model of protein folding.

The mechanism of protein folding has been the subject of extensive investigation during the last decade, both because of its academic challenge and because of its relation to many diseases which are known to occur due to misfolding of proteins. In this context, we report here a systematic investigation on the step-wise formation of a helical structure by the addition of hexafluoroacetone, in a 14-residue peptide derived from a part of the scorpion neurotoxin protein. The NMR and circular dichroism results indicate that the peptide has an inherent propensity for helix formation and this is limited to the internal few residues in aqueous solution. With the addition of the fluorosolvent, the helical content progressively increases and spans the whole sequence. This is accompanied by concomitant packing of the side chains. These results provide support to the so-called hierarchic model of protein folding which dictates that the local sequence determines the secondary structures in the protein and the side chains play an important role in this process.

Acetone↗
PubMed2001

Buthus martensi Karsch agonist of skeletal-muscle RyR-1, a scorpion active polypeptide: antinociceptive effect on rat peripheral nervous system and spinal cord, and inhibition of voltage-gated Na(+) currents in dorsal root ganglion neurons.

The antinociceptive effect and potential antinociceptive mechanism of Buthus martensi Karsch agonist of skeletal-muscle RyR-1 (BmK AS-1), a scorpion venom derived neurotoxic polypeptide, have been investigated in rats. The results show that: (a) the withdrawal latency to rat plantar radiant heat was increased significantly by 100 and 150% after intrathecal injection of 0.6 and 1.2 microg doses; (b) C components of rat nociceptive flexion reflex were reduced to 72, 50 and 29% after intraplantar injection of 5, 10 and 20 microg doses; (c) both central (spinal cord) and peripheral antinociceptive effects of BmK AS-1 could not be reversed by naloxone; (d) tetrodotoxin-resistant (TTX-R) Na(+) current was depressed to 83.87+/-1.64, 64.73+/-5.43 and 15.85+/-17.63%, and tetrodotoxin-sensitive (TTX-S) Na(+) current was depressed to about 81.27+/-2.5, 49.08+/-8.09 and 9.03+/-12.34% with 0.2, 1.0 and 10 microg/ml BmK AS-1 measured using patch clamp recording in rat small dorsal root ganglion (DRG) neurons, respectively. The results indicate that BmK AS-1 may be a new component with potent antinociceptive activity mediated by modulating TTX-S and TTX-R Na(+) channels.

Animals↗
PubMed2002

Molecular determinant of Na(v)1.8 sodium channel resistance to the venom from the scorpion Leiurus quinquestriatus hebraeus.

The scorpion venom from Leiurus quinquestriatus (LQTX) alters the kinetics of tetrodotoxin (TTX)-sensitive channels such as the skeletal muscle sodium channel Na(v)1.4. In this study, we tested the effects of LQTX on the TTX-resistant sodium current generated by Na(v)1.8 channels in sensory neurons. Na(v)1.8 current was found to be resistant to LQTX, whereas LQTX slowed inactivation of the current generated by Na(v)1.4 and induced a persistent current. LQTX has been shown to bind the S3-S4 linker of domain four (D4S3-S4) of rat brain Na(v)1.2 sodium channels. Sequence analysis shows that the D4S3-S4 linker is longer in Na(v)1.8 than in Na(v)1.4 by four amino acids: Serine; Leucine; Glutamic acid; and Aspargine (SLEN). Na(v)1.4-SLEN, a chimera construct carrying SLEN at the analogous position in the D4S3-S4 linker, was also found to be resistant to LQTX. Therefore, we conclude that the tetrapeptide SLEN at the D4S3-S4 linker region is sufficient to make Na(v)1.8 resistant to LQTX.

Action Potentials↗
PubMed2003

Modulation of BmK AS, a scorpion neurotoxic polypeptide, on voltage-gated Na+ channels in B104 neuronal cell line.

The modulation of BmK AS, a neurotoxic polypeptide from scorpion Buthus martensi Karsch, on the voltage-gated Na(+) channels has been investigated in the B104 neuroblastoma cell line by whole-cell patch clamping. It was found that the whole Na(+) currents and tetrodotoxin-resistant Na(+) current were depressed in a biphasic manner and both steady-state activation and inactivation curves were shifted toward the hyperpolarizing direction in the presence of BmK AS. The results suggested that BmK AS could inhibit both tetrodotoxin-sensitive and -resistant Na(+) currents via modulating the gating mechanism of the voltage-gated Na(+) channels in B104 cells.

Animals↗
PubMed2000

Oxygen transport proteins: III. Structural studies of the scorpion (Buthus sindicus) hemocyanin, partial primary structure of its subunit Bsin1.

The hemocyanin (Hc) from Buthus sindicus, studied in the native state, demonstrated to be an aggregate of eight different types of subunits arranged in four cubic hexamers. Both, the 'top' and the 'side' views of the native molecule have been identified from the negatively stained specimens using transmission electron microscopy. Out of these, eight different polypeptide chains, the partial primary structure (68%) of a subunit Bsin1 (Mr = 72422.7 Da) was established using a combination of automated Edman degradation and mass spectrometry. A multiple sequence alignment with other closely related cheliceratan Hc subunits revealed average identities of ca. 60%. Most of the structurally important residues, i.e. copper and calcium-binding ligands, as well as the residues involved in the presumed oxygen entrance pathway, proved to be strictly conserved in Bsin1. Sequence variations have been observed around the functionally important chloride-binding site, not only for the B. sindicus subunit Bsin1, but also for the subunit Aaus-6 of the scorpion A. australis and the subunit Ecal-a from the spider Eurypelma californicum Hcs. Deviation in the primary structure related to the chloride-binding site suggest that the effect of chloride ions may vary in different hemocyanins. Furthermore, the secondary structural contents of the Hc subunit Bsin1 were determined by circular dichroism revealing ca. 33% alpha-helix, 18%, beta-sheet, 19% beta-turn, and 30% random coil composition. These values are in good agreement with the crystal structure of the closely related Hc subunit Lpol-II from horseshoe crab L. polyphemus. Electron microscopic studies of the purified Hc subunit under native conditions revealed that Bsin1 has self aggregation properties. Results of these studies are discussed.

Amino Acid Sequence↗
PubMed2000

Antihyperalgesia effect of BmK IT2, a depressant insect-selective scorpion toxin in rat by peripheral administration.

The study was undertaken to assess the antihyperalgesia effect of BmK IT2, a sodium channel-specific ligand purified from the venom of Chinese scorpion Buthus martensi Karsch in rat by peripheral injection. The peripheral inflammation of rat was induced by carrageenan resulted in hyperalgesia to heat stimulus. The heat hyperalgesia was measured by paw withdrawal latency (PWL). PWL was increased to 272 +/- 18%, 217 +/- 19% and 186 +/- 16% of the control by application of 10 microl BmK IT2 at the concentration of 0.1, 0. 01 and 0.001 mg/ml in inflammatory rats, respectively. In contrast, PWL was enhanced to about 177 +/- 16%, 141 +/- 15% and 133 +/- 15% of the control at the same applied concentrations of BmK IT2 in normal rats. The results thus suggest that BmK IT2 can produce peripheral antihyperalgesia and antinociception, which might be attributed a pathway of modulating the sodium channels on nociceptor.

Analgesics↗
PubMed2002

Dynamic determination and possible mechanism of amino acid transmitter release from rat spinal dorsal horn induced by the venom and a neurotoxin (BmK I) of scorpion Buthus martensi Karsch.

In the present communication, we determined the dynamic release of amino acid transmitters from spinal dorsal horn induced by scorpion Buthus martensi Karsch (BmK) venom and a neurotoxin (BmK I). The results found that glutamate and aspartate release could be evoked significantly within the initial 30 min with the applied doses of either 0.05 and 0.01 mg BmK venom or 0.01 and 0.002 mg BmK I. However, gamma-aminobutyric acid (GABA) release could be largely evoked during the second 30 min by the venom, but not by BmK I. The result suggested that nociceptive afferent fibers could be activated to induce excitatory amino acid release from spinal dorsal horn by nociceptive factors such as BmK I, but the delayed release of GABA might be attributed to the modulating role of some antinociceptive components in the venom.

Animals↗
PubMedDate not supplied

Scorpion BmK venom induces nociceptive response of rats by plantar injection.

In this study, the nociceptive responses induced by subcutaneous injection of scorpion BmK venom into the plantar surface of rat hind paw were quantified. The suitable dose of the venom is between 0.01 and 0.05 mg. The venom injection could induce local edema and tonic-pain responses, which had lasted more than 1 h. The pain scores reached peak intensity within 20 min, and then decreased slowly. Morphine, as a classic analgesic drug, could inhibit the spontaneous nociceptive response induced by the venom. With Morphine pretreatment, the mean pain scores for the entire 60 min were significantly decreased (P<.05). BmK I, a main lethal component, was also found to induce nociceptive responses with dose-dependent means. The nociceptive responses induced by BmK I could be partially inhibited by morphine.

Analgesics, Opioid↗
PubMed1998

Voltage sensor-trapping: enhanced activation of sodium channels by beta-scorpion toxin bound to the S3-S4 loop in domain II.

Polypeptide neurotoxins alter ion channel gating by binding to extracellular receptor sites, even though the voltage sensors are in their S4 transmembrane segments. By analysis of sodium channel chimeras, a beta-scorpion toxin is shown here to negatively shift voltage dependence of activation and enhance closed state inactivation by binding to a receptor site that requires glycine 845 (Gly-845) in the S3-S4 loop at the extracellular end of the S4 segment in domain II of the alpha subunit. Toxin action requires prior depolarization to drive the S4 voltage sensors outward, but these effects are lost in the mutant G845N. The results reveal a voltage sensor-trapping model of toxin action in which the IIS4 voltage sensor is trapped in its outward, activated position by toxin binding.

Amino Acid Sequence↗
PubMed2003

Functional consequences of deleting the two C-terminal residues of the scorpion toxin BmTX3.

We deleted the two C-terminal residues of the scorpion toxin BmTx3, a peptidyl inhibitor of a transient A-type K(+) current in striatum neurons in culture, to assess their contribution to receptor recognition. The sBmTX3-delYP analog was shown to have a native-like structure in one-dimensional 1H-nuclear magnetic resonance (NMR) spectroscopy. We found that sBmTX3-delYP bound to its receptor less efficiently than the wild-type molecule (by a factor of about 10(5)) in binding assays with rat brain membranes, and that this molecule did not block the A-type K(+) current (at a concentration of 35 microM) in whole-cell patch clamp experiments with striatum neurons. Also, these results show that the A-type K(+) channel blocked by BmTX3 should have a canonical K(+) channel pore structure.

Amino Acid Sequence↗