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PubMedDate not supplied

Envenomation by the scorpion Centruroides sculpturatus.

Envenomation by the scorpion C. sculpturatus can be life threatening. The action of the venom is to produce prolonged and excessive firing of neuronal axons which results in a wide variety of signs and symptoms. Records of 670 patients suffering from scorpion stings in central Arizona in 1982 were reviewed to characterize the clinical course of these patients. While adults appear to be stung more often than children, children are more likely to develop a severe illness requiring intensive supportive care. The intravenous administration of specific C. sculpturatus antivenom results in resolution of serious signs and symptoms within minutes, with patients completely asymptomatic within 1 1/2 hours. The administration of antivenom is recommended as the treatment of choice for severe envenomations after the initiation of appropriate supportive care.

Action Potentials↗
PubMed1995

Paresthesia in envenomation by the scorpion Leiurus quinquestriatus.

We observed two patients with systemic paresthesia as the sole systemic manifestation of envenomation by L. quinquestriatus. A prospective study of the incidence of local and systemic paresthesia in 20 consecutive patients stung by this scorpion was done. Sixteen patients (80%) had only local complaints and 4/20 (20%) had mild systemic manifestations. Eleven patients (55%) had local paresthesia and in 2 patients (10%) systemic paresthesia was noted involving all four extremities in one patient and the perioral area in the other. The possible mechanism of paresthesia following a scorpion sting is discussed.

Adult↗
PubMedDate not supplied

Immunity against the venom of Mexican scorpion Centruroides lumpidus limpidus induced by some proteins from this venom.

A protein fraction, which consisted of at least 12 proteins, was obtained from the venom of Mexican scorpion Centruroides limpidus limpidus. The molecular weights of these proteins ranged between 9,800 and 163,000 daltons. This fraction was separated from the rest of the venom components, which were almost all neurotoxins, by chromatographying the venom obtained by electrical stimulation through a Sephadex G-50M column. This fraction was non-toxic for mice, even at dose of 200 micrograms/mouse. The most important is that it was able to induce immunity against C. l. limpidus venom, since 92.8% of the animals inoculated with three doses survived after the challenge with 39.2 micrograms of venom (2 DL50 for mice of 20 g); on the contrary, 88 min after the challenge, 100% of the control mice had already died. In another experiment, this immunogen was inoculated into mice three times at variable doses. Seven days after the last injection, each mouse was challenged with 19.6 micrograms of venom. In all controls the typical envenomation picture produced by scorpion venom was developed, and death was registered in 19% of the animals. In contrast, 87% of mice immunized with the highest dose failed to show signs of envenomation or died throughout the observation time. Only two immunized animals (13%) showed mild tachycardia and hyperpnea at 120 min post-challenge. Immunoelectrophoresis and immunodiffusion tests revealed that these proteins induced antibodies against components of the most toxic fraction.

Animals↗
PubMed1961

Studies of scorpion antivenins. 1. Paraspecificity.

This paper describes neutralization tests conducted to determine the effectiveness of five commercially available antivenins, each from a different geographical area, in neutralizing homologous and heterologous scorpion venoms. Venoms of eight scorpion species were used. The work was undertaken because of current interest in the development of polyvalent antivenins for the treatment of venomous bites and stings, and for determination of paraspecific action of existing antivenins as a first step in such a developmental programme. During the studies described, several instances of cross-protection were found, and in some tests heterologous antivenins were more effective than homologous antivenins in protecting white mice against the effects of venom injections. The results obtained should be of practical value in planning a systematic approach towards production of a polyvalent antivenin for use anywhere in the world.

Animals↗
PubMed1992

Role of atropine in management of cardiovascular manifestations of scorpion envenoming in humans.

We undertook a retrospective analysis of 35 victims of red scorpion (Mesobuthus tamulus) sting, admitted to our hospital in Mahad, Maharashtra State, India. Increase in duration as well as severity of clinical signs, including myocardial injury and poor response to conventional treatment, were observed in 17 victims treated with atropine compared to another 18 victims who were not so treated. We do not advocate routine use of atropine to block transient cholinergic effects of scorpion envenoming.

Adolescent↗
PubMed2003

Enhanced Li+ binding energies in alkylbenzene derivatives: the scorpion effect.

The gas-phase lithium cation basicities (LCBs; Gibbs free energy of binding) of ethyl-, n-butyl-, and n-heptylbenzene have been measured by Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometry. The structures of the corresponding complexes and their relative stabilities were investigated through the use of B3LYP/6-311G(+)(3df,2p)//B3LYP/6-31G(d) density functional theory calculations. For n-butylbenzene and n-heptylbenzene, the most stable adducts correspond to pi complexes in which the alkyl chain coils toward the aromatic ring to favor its interaction with the metal cation. The extra stabilization provided by the flexible alkyl chain polarized by the charge on Li(+) is named the "scorpion effect". Conversely, these coiled conformations are among the least stable in the neutral system; they are not all stationary points on the potential-energy surface. The formation of complexes with a coiled alkyl chain leads to a significant enhancement of the Li(+) bonding energies (LBEs), which are approximately 20-30 kJ mol(-1) higher than those calculated for alkylbenzene pi complexes in which an uncoiled chain remains distant from the cation and thus minimizes the scorpion effect. This enhancement is less significant when LCBs are concerned, because the scorpion effect is entropically disfavored. There is very good agreement between the experimental Li(+) gas-phase basicities and the calculated values, provided that the statistical distribution of the conformers present in the gas phase is taken into account in this calculation.

Journal Article↗
PubMed2005

The mitochondrial genome sequence of the scorpion Centruroides limpidus (Karsch 1879) (Chelicerata; Arachnida).

The mitochondrial genome of the scorpion Centruroides limpidus (Chelicerata; Arachnida) has been completely sequenced and is 14519 bp long. The genome contains 13 protein-encoding genes, two ribosomal RNA genes, 21 transfer RNA genes and a large non-coding region related to the control region. The overall A+T composition is the lowest among the complete mitochondrial sequences published within the Chelicerata subphylum. Gene order and gene content differ slightly from that of Limulus polyphemus (Chelicerata: Xiphosura): i.e., the lack of the trnD gene, and the translocation-inversion of the trnI gene. Preliminary phylogenetic analysis of some Chelicerata shows that scorpions (C. limpidus and Mesobuthus gibbosus) make a tight cluster with the spiders (Arachnida; Araneae). Our analysis does not support that Scorpiones order is the sister group to all Arachnida Class, since it is closer to Araneae than to Acari orders.

Animals↗
PubMed2003

The "SCORPION" experiment onboard the International Space Station. Preliminary results.

The "SCORPION" program onboard the Russian Segment (RS) of the International Space Station (ISS) is designed to carry out complex research of the effects of the nar-Earth space parameters on the conditions under which various experiments and operations are being conducted. Special attention in this program was paid to the biological objects onboard the orbital station, e.g. it was found that variation in the number of colony forming units (micromicets and bacteria) correlates with the solar activity and the absorbed dose. The "SCORPION" experiment onboard the RS ISS started in January 2002. It was designed to measure the following parameters inside the space absorbed doses in different places inside the RS ISS, the fluxes of energetic charged particles, neutrons and gamma-quanta; the vectors of the magnetic field and low-frequency electromagnetic waves. At the same time the growth of micromicets on the samples of various materials was studied. The description of the "SCORPION" experiment and the preliminary results obtained onboard the RS ISS in 2002 are presented.

Aspergillus niger↗
PubMed1997

NMR solution structure of a two-disulfide derivative of charybdotoxin: structural evidence for conservation of scorpion toxin alpha/beta motif and its hydrophobic side chain packing.

The alpha/beta scorpion fold consisting of a short alpha-helix and beta-sheet is a structural motif common to scorpion toxins, insect defensins, and plant gamma-thionins that invariably contains three disulfides. CHABII is a two-disulfide derivative of the scorpion toxin charybdotoxin (ChTX), chemically synthesized by inserting two L-alpha-aminobutyric acids in place of the two half-cystine residues involved in the disulfide 13-33. This disulfide is one of the two disulfides which connect the alpha-helix to the beta-sheet. The solution structure of CHABII was determined at pH 6.3 and 5 degrees C using 2D NMR and simulated annealing from 513 distance and 46 dihedral angle constraints. The NMR structure of CHABII is well-defined as judged from the low value of the averaged backbone rms deviation between the 30 lowest energy structures and the energy-minimized mean structure ((rmsd) = 0.65 A for the entire sequence and 0.48 A for the segment 3-36). Analysis and comparison of the solution structures of CHABII and ChTX lead to the following conclusions: (i) the fold of CHABII is similar to that of ChTX as indicated by the low value of the averaged backbone atomic rms deviation between the 10 lowest energy solution structures of the two proteins (1.44 A); (ii) the packing of the hydrophobic core is well-preserved, underlying the critical structural role of the hydrophobic interactions even for such a small and cysteine-rich protein as ChTX.

Amino Acid Sequence↗
PubMed2006

Janus scorpionates: supramolecular tectons for the directed assembly of hard-soft alkali metallopolymer chains.

A new scorpionate ligand [HB(mtda)3-] containing mercaptothiadiazolyl (mtda) heterocyclic rings with both hard nitrogen donors and soft sulfur donors has been prepared. This new ligand, the Janus scorpionate, is a hybrid of a tris(pyrazolyl)borate and a tris(mercaptoimidazolyl)borate. The differential hard/soft character of the dissimilar donor groups in this bridging ligand was exploited for the controlled solid-state organization of homometallic and heterometallic alkali metal coordination polymers. Remarkably, in the case of sodium, coordination polymers with both acentric (with NaS3N3H kernels) and centric (with alternating NaN6 and NaS6H2 kernels) chains are found in the same crystal (where the centricity is defined by the relative orientations of the B-H bonds of the ligands along the lattice). For the homometallic potassium congener, the larger cation size, compared to sodium, induced significant distortions and favored a polar arrangement of ligands in the resulting coordination polymer chain. An examination of the solid-state structure of the mixed alkali metal salt system revealed that synergistic binding of smaller sodium cations to the nitrogen portion and of the larger potassium cations to the sulfur portion of the ligand minimizes the ligand distortions relative to the homometallic coordination polymer counterparts, a design feature of the ligand that likely assists in thermodynamically driving the self-assembly of the heterometallic chains. The effect of alkali metal complexation on the solution properties of the ligand was studied by comparing NMR chemical shifts, B-H stretching frequencies, and electrochemical properties with those of the noncoordinating tetrabutylammonium salt of the scorpionate. The similarity of these data regardless of cation indicates that the salts are likely dissociated in solution rather than maintaining their solid-state polymeric structures. This data is augmented by the ESI(+/-) mass spectral data for a series of mixed alkali metal tris(mercaptothiadiazolyl)borates that also indicate that dissociation occurs in solution.

Journal Article↗
PubMed2006

Very small and soft scorpionates: water stable technetium tricarbonyl complexes combining a bis-agostic (k(3)-H, H, S) binding motif with pendant and integrated bioactive molecules.

The novel trihydro(mercaptoazolyl)borates Na[H(3)B(tim(Me))] (L(1)) (tim(Me) = 2-mercapto-1-methylimidazolyl), Na[H(3)B(tim(Bupip))] (L(2)) (tim(Bupip) = 1-[4-((2-methoxyphenyl)-1-piperazinyl)butyl]-2-mercaptoimidazolyl), and Na[H(3)B(bzt)] (L(3)) (bzt = 2-mercaptobenzothiazolyl) were synthesized by reaction of NaBH(4) with the corresponding azole. Ligands L(1)-L(3) represent a new class of light and soft scorpionates that stabilizes the [M(CO)(3)](+) core (M = (99)Tc, Re) by formation of the complexes fac-[M{kappa(3)-H(mu-H)(2)B(tim(Me))}(CO)(3)] (M = (99)Tc (1), Re (2)), fac-[Re{kappa(3)-H(mu-H)(2)B(tim(Bupip))}(CO)(3)] (3), and fac-[Re{kappa(3)-H(mu-H)(2)B(bzt)}(CO)(3)] (4), respectively. The soft scorpionates are coordinated to the metal in unique (kappa(3)-H, H', S) fashion, as confirmed by X-ray crystallography of 1, 2, and 4. These complexes with bis-agostic hydride coordination are formed in aqueous solution with the two hydrides replacing two coordinating aquo ligands. The agostic hydrogen atoms were located directly, confirming an unprecedented donor atom set combining one sulfur and two hydrogen atoms. Preliminary studies have shown the possibility of preparing some of these complexes at the no carrier added level ((99m)Tc), under conditions as required in radiopharmaceutical preparation. Due to their lipophilicity, small-size, and easy functionalization with adequate biomolecules, the trihydro(mercaptoazolyl)borate technetium tricarbonyl complexes are suitable for the design of CNS receptor ligand radiopharmaceuticals as exemplified with 3, comprising a pendant serotonergic 5-HT(1A) ligand. The integrated design of radiopharmaceuticals involving a bis-agostic scorpionate ligand is demonstrated by the synthesis of 4, with an integrated benzothiazolyl fragment for the recognition of beta-amyloid plaques.

Journal Article↗
PubMed2001

Duplex Scorpion primers in SNP analysis and FRET applications.

Scorpions are fluorogenic PCR primers with a probe element attached at the 5'-end via a PCR stopper. They are used in real-time amplicon-specific detection of PCR products in homogeneous solution. Two different formats are possible, the 'stem-loop' format and the 'duplex' format. In both cases the probing mechanism is intramolecular. We have shown that duplex Scorpions are efficient probes in real-time PCR. They give a greater fluorescent signal than stem-loop Scorpions due to the vastly increased separation between fluorophore and quencher in the active form. We have demonstrated their use in allelic discrimination at the W1282X locus of the ABCC7 gene and shown that they can be used in assays where fluorescence resonance energy transfer is required.

DNA Primers↗
PubMed2006

Real-time PCR detection and speciation of Cryptosporidium infection using Scorpion probes.

At least eight species of Cryptosporidium can cause human infection and disease. A real-time PCR (qPCR) assay based on the 18S rRNA gene and utilizing a Scorpion probe was developed to detect all human-pathogenic Cryptosporidium without the usual need for nested amplification. Sensitivity of detection in stool samples was highest using a glass bead-based DNA extraction method (under 10(3) oocysts per stool sample). The assay was validated against 123 human stool specimens from Bangladesh and Tanzania, exhibited a sensitivity and specificity of >91% versus microscopy, and detected an additional eight microscopy-negative infections. Cryptosporidium parvum-specific and Cryptosporidium meleagridis-specific Scorpion qPCR assays that provided 100% accurate speciation compared with VspI RFLP analysis and sequencing were developed subsequently. These Scorpion probe qPCR assays are simpler to perform than existing nested PCR and RFLP methods for diagnosis and epidemiological investigation of cryptosporidiosis.

Animals↗
PubMed1999

A scorpion alpha-like toxin that is active on insects and mammals reveals an unexpected specificity and distribution of sodium channel subtypes in rat brain neurons.

Several scorpion toxins have been shown to exert their neurotoxic effects by a direct interaction with voltage-dependent sodium channels. Both classical scorpion alpha-toxins such as Lqh II from Leiurus quiquestratus hebraeus and alpha-like toxins as toxin III from the same scorpion (Lqh III) competitively interact for binding on receptor site 3 of insect sodium channels. Conversely, Lqh III, which is highly toxic in mammalian brain, reveals no specific binding to sodium channels of rat brain synaptosomes and displaces the binding of Lqh II only at high concentration. The contrast between the low-affinity interaction and the high toxicity of Lqh III indicates that Lqh III binding sites distinct from those present in synaptosomes must exist in the brain. In agreement, electrophysiological experiments performed on acute rat hippocampal slices revealed that Lqh III strongly affects the inactivation of voltage-gated sodium channels recorded either in current or voltage clamp, whereas Lqh II had weak, or no, effects. In contrast, Lqh III had no effect on cultured embryonic chick central neurons and on sodium channels from rat brain IIA and beta1 subunits reconstituted in Xenopus oocytes, whereas sea anemone toxin ATXII and Lqh II were very active. These data indicate that the alpha-like toxin Lqh III displays a surprising subtype specificity, reveals the presence of a new, distinct sodium channel insensitive to Lqh II, and highlights the differences in distribution of channel expression in the CNS. This toxin may constitute a valuable tool for the investigation of mammalian brain function.

Animals↗
PubMed1997

Solution structure of TsKapa, a charybdotoxin-like scorpion toxin from Tityus serrulatus with high affinity for apamin-sensitive Ca(2+)-activated K+ channels.

TsKapa (TsK), purified from the Buthidae Tityus serrulatus is a very high potent ligand for small-conductance apamin-sensitive calcium-activated potassium channels (SK). It is able to efficiently compete with apamin for binding on this channel (K0.5 = 0.3 nM) [Legros, C. et al., FEBS Lett. 390:81-84, 1996]. The solution structure of TsK has been determined by 2D-NMR techniques, which led to the full description of its 3D conformation: a short alpha helix from residues 14 to 20 and a three-stranded antiparallel beta sheet (residues 2-3, 27-29, and 32-34). The interaction of TsK with the SK potassium channel has been modeled according to the charge anisotropy of the ligand. The resulting dipole moment orientates TsK so that it presents toward the receptor, a surface, mainly basic, encompassing residues K18 and K19 on one side and R9 and Y8 on the other. Despite its three-dimensional structure that is related with scorpion toxins active on voltage-gated potassium channels such as charybdotoxin, the pharmacological activity and specificity of TsK is related with shorter scorpion toxins (i.e., possessing an only two-stranded beta sheet) such as scyllatoxin (also named leiurotoxin I) or P05.

Amino Acid Sequence↗
PubMed2006

Proteomic analysis of Tityus discrepans scorpion venom and amino acid sequence of novel toxins.

The Venezuelan scorpion Tityus discrepans is known to cause human fatalities. We describe the first complete proteomic analysis of its venom. By HPLC 58 different fractions were obtained and 205 different components were identified by MS analysis. Components having molecular masses from 272 to 57 908 amu were found. Forty homogeneous components had their N-terminal amino acid sequence determined by Edman degradation, from which two new peptides named TdK2 and TdK3 (meaning T. discrepans (Td) K(+) channel toxins 2 and 3) were fully characterized. The first contains 34 amino acid residues with a molecular mass of 3451 amu, and the second has 36 amino acids with 3832 amu. Both peptides are tightly bound by three disulfide bridges. TdK2 was shown to block reversibly the Shaker B K(+)-channel expressed heterologously in Sf9 cells. The systematic number assigned to TdK2 is alpha-KTx-18.2 and that of TdK3 is alpha-KTx-18.3. Comparative analysis of the amino acid sequences found suggests that this venom contains peptides highly similar to those that block K(+) channels, as well as those that modify the gating mechanisms of Na(+) channels, found in other scorpions. Additionally, peptides similar to defensins were also identified.

Amino Acid Sequence↗
PubMed2005

The solution structure of BmTx3B, a member of the scorpion toxin subfamily alpha-KTx 16.

This article reports the solution structure of BmTx3B (alpha-KTx16.2), a potassium channel blocker belonging to the subfamily alpha-KTx16, purified from the venom of the Chinese scorpion Buthus martensi Karsch. In solution, BmTx3B assumes a typical CSalphabeta motif, with an alpha-helix connected to a triple-stranded beta-sheet by 3 disulfide bridges, which belongs to the first structural group of short-chain scorpion toxins. On the other hand, BmTx3B is quite different from other toxins (such as ChTx and AgTx2) of this group in terms of the electrostatic and hydrophobic surface distribution. The functional surface (beta-face) of the molecule is characterized by less basic residues (only 2: Lys28 and Arg35) and extra aromatic residues (Phe1, Phe9, Trp15, and Tyr37). The peptide shows a great preference for the Kca1.1 channel over the Kv channel (about a 10(3)-fold difference). The model of BmTx3B/Kca1.1 channel complex generated by docking and dynamic simulation reveals that the stable binding between the BmTx3B and Kca1.1 channel is favored by a number of aromatic pi-pi stacking interactions. The influences of these structural features on the kinetic behavior of the toxin binding to Kca1.1 channel are also discussed.

Amino Acid Sequence↗
PubMed2004

First chemical synthesis of a scorpion alpha-toxin affecting sodium channels: the Aah I toxin of Androctonus australis hector.

Aah I is a 63-residue alpha-toxin isolated from the venom of the Buthidae scorpion Androctonus australis hector, which is considered to be the most dangerous species. We report here the first chemical synthesis of Aah I by the solid-phase method, using a Fmoc strategy. The synthetic toxin I (sAah I) was renatured in DMSO-Tris buffer, purified and subjected to thorough analysis and comparison with the natural toxin. The sAah I showed physico-chemical (CD spectrum, molecular mass, HPLC elution), biochemical (amino-acid composition, sequence), immunochemical and pharmacological properties similar to those of the natural toxin. The synthetic toxin was recognized by a conformation-dependent monoclonal anti-Aah I antibody, with an IC50 value close to that for the natural toxin. Following intracerebroventricular injection, the synthetic and the natural toxins were similarly lethal to mice. In voltage-clamp experiments, Na(v) 1.2 sodium channel inactivation was inhibited by the application of sAah I or of the natural toxin in a similar way. This work describes a simple protocol for the chemical synthesis of a scorpion alpha-toxin, making it possible to produce structural analogues in time.

Animals↗