The Experts below are selected from a list of 924 Experts worldwide ranked by ideXlab platform
Pierre E. Bougis - One of the best experts on this subject based on the ideXlab platform.
-
Serotherapy against Voltage-Gated Sodium Channel-Targeting αToxins from Androctonus Scorpion Venom
MDPI AG, 2019Co-Authors: Marie-france Martin-eauclaire, Fatima Laraba-djebari, Sonia Adi-bessalem, Djelila Hammoudi-triki, Pierre E. BougisAbstract:Because of their venom lethality towards mammals, scorpions of the Androctonus genus are considered a critical threat to human health in North Africa. Several decades of exploration have led to a comprehensive inventory of their venom components at chemical, pharmacological, and immunological levels. Typically, these venoms contain selective and high affinity ligands for the voltage-gated sodium (Nav) and potassium (Kv) channels that dictate cellular excitability. In the well-studied Androctonus australis and Androctonus mauretanicus venoms, almost all the lethality in mammals is due to the so-called α-toxins. These peptides commonly delay the fast inactivation process of Nav channels, which leads to increased sodium entry and a subsequent cell membrane depolarization. Markedly, their neutralization by specific antisera has been shown to completely inhibit the venom’s lethal activity, because they are not only the most abundant venom peptide but also the most fatal. However, the structural and antigenic polymorphisms in the α-toxin family pose challenges to the design of efficient serotherapies. In this review, we discuss past and present accomplishments to improve serotherapy against Androctonus scorpion stings
-
The scorpion toxin Bot IX is a potent member of the α-like family and has a unique N-terminal sequence extension
FEBS Letters, 2016Co-Authors: Marie-france Martin-eauclaire, Juan Salvatierra, Frank Bosmans, Pierre E. BougisAbstract:We report the detailed chemical, immunological and pharmacological characterization of the α-toxin Bot IX from the Moroccan scorpion Buthus occitanus tunetanus venom. Bot IX, which consists of 70 amino acids, is a highly atypical toxin. It carries a unique N-terminal sequence extension and is highly lethal in mice. Voltage clamp recordings on oocytes expressing rat Nav1.2 or insect BgNav1 reveal that, similar to other α-like toxins, Bot IX inhibits fast inactivation of both variants. Moreover, Bot IX belongs to the same structural/immunological group as the α-like toxin Bot I. Remarkably, radioiodinated Bot IX competes efficiently with the classical α-toxin AaH II from Androctonus australis, and displays one of the highest affinities for Nav channels.
-
Androctonus toxins targeting voltage gated sodium channels
2013Co-Authors: Mariefrance Martineauclaire, Brigitte Céard, Jean-pierre Rosso, Najwa Abbas, Pierre E. BougisAbstract:The Androctonus genus constitutes a serious threat to human health in Northern Africa and Southwest Asia because some of the Androctonus subspecies produce the most dangerous venoms for mammals. These venoms have provided several high selective affinity ligands, which specifically interact with sodium, potassium, chloride, and calcium channels. However, the vast majority of lethal toxins, even present in the venom at few percent, is active on voltage-gated sodium (Nav) channels and is responsible of almost the whole venom toxicity in mice by subcutaneous injection. During the last four decades, an increasing amount of data was published on the isolation, chemical, pharmacological, and immunological characterization of several structurally distinct families of these extremely active Androctonus toxins, which induce different biological answers when applied to Nav channels. These toxins have been further extensively used to study the functioning and decipher the topology of Nav channels. This chapter M.-F. Martin-Eauclaire (*) • N. Abbas • B. Ceard • J.-P. Rosso • P.E. Bougis (*) Aix Marseille Universite, CNRS, CRN2M UMR7286, Marseille, France e-mail: marie-france.eauclaire@univ-amu.fr; pierre-edouard.bougis@univ-amu.fr # Springer Science+Business Media Dordrecht 2015 P. Gopalakrishnakone et al. (eds.), Scorpion Venoms, Toxinology, DOI 10.1007/978-94-007-6404-0_28 441 reviews the current knowledge on Androctonus toxins active on Nav channels only, at the structural, biological, and immunological level. The organization of their gene and mRNA precursor will also be approached.
-
Potassium Channels Blockers from the Venom of Androctonus mauretanicus mauretanicus
Journal of toxicology, 2012Co-Authors: Marie-france Martin-eauclaire, Pierre E. BougisAbstract:K(+) channels selectively transport K(+) ions across cell membranes and play a key role in regulating the physiology of excitable and nonexcitable cells. Their activation allows the cell to repolarize after action potential firing and reduces excitability, whereas channel inhibition increases excitability. In eukaryotes, the pharmacology and pore topology of several structural classes of K(+) channels have been well characterized in the past two decades. This information has come about through the extensive use of scorpion toxins. We have participated in the isolation and in the characterization of several structurally distinct families of scorpion toxin peptides exhibiting different K(+) channel blocking functions. In particular, the venom from the Moroccan scorpion Androctonus mauretanicus mauretanicus provided several high-affinity blockers selective for diverse K(+) channels (SK(Ca), K(v)4.x, and K(v)1.x K(+) channel families). In this paper, we summarize our work on these toxin/channel interactions.
-
New analysis of the toxic compounds from the Androctonus mauretanicus mauretanicus scorpion venom
Toxicon : official journal of the International Society on Toxinology, 2007Co-Authors: Naoual Oukkache, Noreddine Ghalim, Jean-pierre Rosso, Pierre E. Bougis, Meriem Alami, Rachid Saïle, Mohammed Hassar, Marie-france Martin-eauclaireAbstract:Abstract 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.
Marie-france Martin-eauclaire - One of the best experts on this subject based on the ideXlab platform.
-
Serotherapy against Voltage-Gated Sodium Channel-Targeting αToxins from Androctonus Scorpion Venom
MDPI AG, 2019Co-Authors: Marie-france Martin-eauclaire, Fatima Laraba-djebari, Sonia Adi-bessalem, Djelila Hammoudi-triki, Pierre E. BougisAbstract:Because of their venom lethality towards mammals, scorpions of the Androctonus genus are considered a critical threat to human health in North Africa. Several decades of exploration have led to a comprehensive inventory of their venom components at chemical, pharmacological, and immunological levels. Typically, these venoms contain selective and high affinity ligands for the voltage-gated sodium (Nav) and potassium (Kv) channels that dictate cellular excitability. In the well-studied Androctonus australis and Androctonus mauretanicus venoms, almost all the lethality in mammals is due to the so-called α-toxins. These peptides commonly delay the fast inactivation process of Nav channels, which leads to increased sodium entry and a subsequent cell membrane depolarization. Markedly, their neutralization by specific antisera has been shown to completely inhibit the venom’s lethal activity, because they are not only the most abundant venom peptide but also the most fatal. However, the structural and antigenic polymorphisms in the α-toxin family pose challenges to the design of efficient serotherapies. In this review, we discuss past and present accomplishments to improve serotherapy against Androctonus scorpion stings
-
The scorpion toxin Bot IX is a potent member of the α-like family and has a unique N-terminal sequence extension
FEBS Letters, 2016Co-Authors: Marie-france Martin-eauclaire, Juan Salvatierra, Frank Bosmans, Pierre E. BougisAbstract:We report the detailed chemical, immunological and pharmacological characterization of the α-toxin Bot IX from the Moroccan scorpion Buthus occitanus tunetanus venom. Bot IX, which consists of 70 amino acids, is a highly atypical toxin. It carries a unique N-terminal sequence extension and is highly lethal in mice. Voltage clamp recordings on oocytes expressing rat Nav1.2 or insect BgNav1 reveal that, similar to other α-like toxins, Bot IX inhibits fast inactivation of both variants. Moreover, Bot IX belongs to the same structural/immunological group as the α-like toxin Bot I. Remarkably, radioiodinated Bot IX competes efficiently with the classical α-toxin AaH II from Androctonus australis, and displays one of the highest affinities for Nav channels.
-
Neuropathophysiological effect and immuno-inflammatory response induced by kaliotoxin of Androctonus scorpion venom.
Neuroimmunomodulation, 2012Co-Authors: Amina Ladjel-mendil, Marie-france Martin-eauclaire, Fatima Laraba-djebariAbstract:Objective: Kaliotoxin (KTX) is a neurotoxin purified from Androctonus scorpion venom. Purification and pharmacological and immunological charac
-
Potassium Channels Blockers from the Venom of Androctonus mauretanicus mauretanicus
Journal of toxicology, 2012Co-Authors: Marie-france Martin-eauclaire, Pierre E. BougisAbstract:K(+) channels selectively transport K(+) ions across cell membranes and play a key role in regulating the physiology of excitable and nonexcitable cells. Their activation allows the cell to repolarize after action potential firing and reduces excitability, whereas channel inhibition increases excitability. In eukaryotes, the pharmacology and pore topology of several structural classes of K(+) channels have been well characterized in the past two decades. This information has come about through the extensive use of scorpion toxins. We have participated in the isolation and in the characterization of several structurally distinct families of scorpion toxin peptides exhibiting different K(+) channel blocking functions. In particular, the venom from the Moroccan scorpion Androctonus mauretanicus mauretanicus provided several high-affinity blockers selective for diverse K(+) channels (SK(Ca), K(v)4.x, and K(v)1.x K(+) channel families). In this paper, we summarize our work on these toxin/channel interactions.
-
New analysis of the toxic compounds from the Androctonus mauretanicus mauretanicus scorpion venom
Toxicon : official journal of the International Society on Toxinology, 2007Co-Authors: Naoual Oukkache, Noreddine Ghalim, Jean-pierre Rosso, Pierre E. Bougis, Meriem Alami, Rachid Saïle, Mohammed Hassar, Marie-france Martin-eauclaireAbstract:Abstract 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.
Mariefrance Martineauclaire - One of the best experts on this subject based on the ideXlab platform.
-
Androctonus toxins targeting voltage gated sodium channels
2013Co-Authors: Mariefrance Martineauclaire, Brigitte Céard, Jean-pierre Rosso, Najwa Abbas, Pierre E. BougisAbstract:The Androctonus genus constitutes a serious threat to human health in Northern Africa and Southwest Asia because some of the Androctonus subspecies produce the most dangerous venoms for mammals. These venoms have provided several high selective affinity ligands, which specifically interact with sodium, potassium, chloride, and calcium channels. However, the vast majority of lethal toxins, even present in the venom at few percent, is active on voltage-gated sodium (Nav) channels and is responsible of almost the whole venom toxicity in mice by subcutaneous injection. During the last four decades, an increasing amount of data was published on the isolation, chemical, pharmacological, and immunological characterization of several structurally distinct families of these extremely active Androctonus toxins, which induce different biological answers when applied to Nav channels. These toxins have been further extensively used to study the functioning and decipher the topology of Nav channels. This chapter M.-F. Martin-Eauclaire (*) • N. Abbas • B. Ceard • J.-P. Rosso • P.E. Bougis (*) Aix Marseille Universite, CNRS, CRN2M UMR7286, Marseille, France e-mail: marie-france.eauclaire@univ-amu.fr; pierre-edouard.bougis@univ-amu.fr # Springer Science+Business Media Dordrecht 2015 P. Gopalakrishnakone et al. (eds.), Scorpion Venoms, Toxinology, DOI 10.1007/978-94-007-6404-0_28 441 reviews the current knowledge on Androctonus toxins active on Nav channels only, at the structural, biological, and immunological level. The organization of their gene and mRNA precursor will also be approached.
-
expanding the scorpion toxin α ktx 15 family with ammtx3 from Androctonus mauretanicus
FEBS Journal, 2002Co-Authors: Helene Vacher, Lourival D. Possani, Pierre E. Bougis, Meriem Alami, Marcel Crest, Mariefrance MartineauclaireAbstract:A novel toxin, AmmTX3 (3823.5 Da), was isolated from the venom of the scorpion Androctonus mauretanicus. It showed 94% sequence homology with Aa1 from Androctonus australis and 91% with BmTX3 from Buthus martensi which, respectively, block A-type K+ current in cerebellum granular cells and striatum cultured neurons. Binding and displacement experiments using rat brain synaptosomes showed that AmmTX3 and Aa1 competed effectively with 125I-labelled sBmTX3 binding. They fully inhibited the 125I-labelled sBmTX3 binding (Ki values of 19.5 pm and 44.2 pm, respectively), demonstrating unambiguously that the three molecules shared the same target in rat brain. The specific binding parameters of 125I-labelled AmmTX3 for its site were determined at equilibrium (Kd = 66 pm, Bmax = 22 fmol per mg of protein). Finally, patch-clamp experiments on striatal neurons in culture demonstrated that AmmTX3 was able to inhibit the A-type K+ current (Ki = 131 nm).
-
characterisation of the gene encoding the α toxin amm v from the scorpion Androctonus mauretanicus mauretanicus
Toxicon, 2001Co-Authors: Meriem Alami, Brigitte Céard, Christian Legros, Pierre E. Bougis, Lhoucine Ouafik, Mariefrance MartineauclaireAbstract:The full-length cDNA encoding the scorpion α-toxin Amm V was amplified from a cDNA library produced from the venom glands of the scorpion Androctonus mauretanicus mauretanicus from Morocco. We deduced the amino acid sequence of the encoded precursor protein and found that the mature toxin was similar to the previously characterised toxin. The genomic DNA sequence encoding the toxin was also amplified, subcloned and sequenced. This also led to the isolation of a new Amm V related-gene. Then, for the first time, we studied changes in the level of toxin mRNA synthesis over time.
-
characterization of a new leiurotoxin i like scorpion toxin po5 from Androctonus mauretanicus mauretanicus
FEBS Letters, 1993Co-Authors: H Zerrouk, A Benslimane, Pascal Mansuelle, H Rochat, Mariefrance MartineauclaireAbstract:Three novel peptide inhibitors of the SKCa channels were purified to homogeneity from the venom of the scorpion Androctonus mauretanicus mauretanicus using one step of RP-HPLC and competition assays with [125I]apamin to rat brain synaptosomes. POi, PO2 and PO5 have K0.5 of 100,100 and 0.02 nM, respectively, for the apamin binding site. The sequence of PO5 was established and compared to that of other scorpion toxins active on K+ channels: it contains 31 residues and has a free carboxyl end. It shares sequence similarity with apamin and leiurotoxin I.
-
analysis by high performance liquid chromatography of Androctonus mauretanicus mauretanicus black scorpion venom
Toxicon, 1991Co-Authors: H Zerrouk, Brigitte Céard, P E Bougis, A Benslimane, Mariefrance MartineauclaireAbstract:Abstract Analysis by high-performance liquid chromatography of Androctonus mauretanicus mauretanicus (black scorpion) venom. Toxicon 29, 951–960, 1991.—The venom of the black scorpion, Androctonus mauretanicus mauretanicus , was obtained by means of manual stimulation and was analyzed using high-performance liquid chromatography. Starting from 20 mg of venom and using only two chromatographic steps, six toxins were purified to homogeneity. They have been characterized by their amino acid content and compared to those already isolated from a pool of venoms obtained using electric stimulation ( Rosso and Rochat , Toxicon 23, 113–125, 1985). The toxins Amm I and Amm II were not found, suggesting either different levels of toxin expression or the existence of Androctonus mauretanicus mauretanicus subspecies. Using rat brain synaptosomes, it was demonstrated that the toxins Amm III, Amm IV and Amm V were α-toxins. The toxin Amm VI was neither α- or β-toxin. Unexpectedly, the toxin Amm VII was found to be a β-toxin, the first one identified in a north African scorpion venom. In addition, some toxins active on mammals exhibited different levels of specificity towards phylogenetically related groups of arthropods.
S. Adiguzel - One of the best experts on this subject based on the ideXlab platform.
-
evaluation of the neutralizing capacity of Androctonus crassicauda olivier 1807 antivenom against leiurus quinquestriatus ehrenberg 1928 venom scorpiones buthidae
Journal of Venomous Animals and Toxins Including Tropical Diseases, 2008Co-Authors: Ozcan Ozkan, Bora Inceoglu, Jozsef Lango, Mustafa Ertek, S. Adiguzel, Bruce D. HammockAbstract:The two most venomous species of the family Buthidae, Leiurus quinquestriatus and Androctonus crassicauda, are found in Africa and in the Middle East. Potency and paraspecific activities of A. crassicauda antivenom (RSHC anti-Ac) were tested against L. quinquestriatus venom. The sera produced by Refik Saydam Hygiene Center (RSHC) showed strong reactivity against the venoms of A. crassicauda and L. quinquestriatus in western blotting and dot-blot analysis. RSHC anti-Ac presents immunoactivity and neutralizing potential against Leiurus quinquestriatus venom. Neutralization capacity of antivenom was found to be 400 µL against 40 minimum lethal doses (MLD) of A. crassicauda scorpion venom and 10 MLD of L. quinquestriatus venom. This study indicates that the RSHC anti-Ac could be used for treating L. quinquestriatus stings.
-
determination of potency and paraspecific effects of Androctonus crassicauda olivier 1807 antivenom against mesobuthus gibbosus brulle 1832 venom scorpiones buthidae
Journal of Venomous Animals and Toxins Including Tropical Diseases, 2007Co-Authors: O. Ozkan, S. Adiguzel, S. Yakistiran, Sirri Kar, Y Cesaretli, Kadri Zafer KaraerAbstract:Scorpion envenomation remains a real health problem in many countries. In scorpionism cases, it is often recommended that patients be treated with species-specific antivenom. Androctonus crassicauda venom has been used as antigen for antivenom production in Turkey, where this antivenom, called Turkish antivenom, has also been effective in the treatment of envenomation caused by species other than A. crassicauda. The present study aimed at determining the paraspecific effects and potency of the Turkish antivenom against Mesobuthus gibbosus (Brulle, 1832) venom. To assess the venom toxicity and the antivenom efficacy, we determined the Minimum Lethal Dose (MLD) and the Minimum Effective Dose (MED) instead of LD50 and ED50, respectively. Androctonus crassicauda antivenom was capable of neutralizing M. gibbosus venom (20 MLD). This was the first study indicating that A. crassicauda antivenom can be used for the treatment of Mesobuthus gibbosus stings, especially in Aegean Region, Turkey.
-
effects of Androctonus crassicauda olivier 1807 scorpiones buthidae venom on rats correlation among acetylcholinesterase activities and electrolytes levels
Journal of Venomous Animals and Toxins Including Tropical Diseases, 2007Co-Authors: Ozcan Ozkan, S. Adiguzel, S. Yakistiran, Sirri Kar, Y Cesaretli, M Kurt, Mehmet Orman, Zafer KaraerAbstract:Scorpions can be considered living fossils because they have changed so little during the last 400 million years. They are venomous arthropods of the Arachnida class and regarded as relatives of spiders, ticks and mites. The aim of the present study was to evaluate the toxicity of Androctonus crassicauda (Olivier, 1807) venom and its effects on the acetylcholinesterase (AchE) activity and on electrolytes levels in rats. Animals were divided into seven groups of five rats each. Test groups received 250µg/kg of venom solution while control group was treated with 200µl of physiological saline solution (PSS). Blood samples were collected from the animals on the 1st, 2nd 4th, 8th, 12th, and 24th hours after subcutaneous injection of venom. Animals were monitored for 24 hours. Androctonus crassicauda venom significantly reduced AchE activity on the 12th hour when compared with control group. A statistically negative correlation between Na+ and K+ (p<0.05) and a positive correlation between Na+ and CL- (p<0.001) ions levels were observed after the administration of A. crassiccauda venom to rats. We can conclude that the differences in the electrolytes levels are due to acute renal failure, since elimination of toxin occurs primarily via the kidney.
-
Study of the relationship between Androctonus crassicauda (Oliver, 1807; scorpiones, buthidae) venom toxicity and telson size, weight and storing condition
Journal of Venomous Animals and Toxins including Tropical Diseases, 2006Co-Authors: O. Ozkan, S. Adiguzel, S. Yakistiran, Ayhan FilaziAbstract:Scorpions are included in the order Scorpiones; class Arachnida. Lethal scorpions are mostly of the Buthidae family. Among these, species belonging to Androctonus, Leiurus and Mesobuthus genera cause most scorpion envenomations in Turkey. This study was performed aiming the production of antivenom by using Androctonus crassicauda telsons. Venom toxicity is related to telson weight, size, and storing condition (open or closed). Telsons of A. crassicauda were collected in Southeastern Anatolia (especially in Harran town, Sanliurfa), Turkey. They were separated according to weight, size, and storing condition - open (a) and closed (b). Venom solution was prepared by maceration of telsons. Swiss albino mice were used to determine the lethal dose 50% (LD50), which was as follows: Group 1a - 2.31mg; Group 1b - 2.66mg; Group 2a - 2.32mg; Group 2b - 2.66mg; Group 3a - 6.66mg; Group 3b - 6.88mg. Among the groups of telsons, the first and the second groups showed different characteristics. However, there were no differences between their toxicity. In the third group, a fourfold amount of telsons was used for toxicity. In other words, telsons weighting from 19.99 to 20mg (first group) and from 29.99 to 30mg (second group) presented similar LD50 values, and telsons weighting from 10 to 19.99mg (third group) showed a fourfold higher LD50 value. This difference was caused by the maturity of scorpions and venom toxicity was related to their size. The first and second groups were considered to be mature and the third group, not adult. Therefore, we can conclude that obtaining open telsons due to environmental factors was not effective for venom toxicity.
-
parametric values of Androctonus crassicauda oliver 1807 scorpiones buthidae from turkey
Journal of Venomous Animals and Toxins Including Tropical Diseases, 2006Co-Authors: Ozcan Ozkan, S. Adiguzel, Sirri KarAbstract:The aim of the present study was to analyze the parametric values of Androctonus crassicauda (Oliver, 1807), the most significant scorpion species in Turkey. For this purpose, 11 male and 11 female A. crassicauda specimens were collected from Sanliurfa region. The body parts most important for species identification were measured by using sensitive calipers. Differences between sexes were statistically significant for pectinal organ length (female: 7.50±1.26mm;male: 8.63±1.05mm; p=0.033), pectinal tooth count (female: 25.36±0.86;male: 33.36±0.80; p=0.000), and carapace width (female: 10.27±1.19mm;male: 9.09±0.73mm; p=0.000). However, body length (female: 90.09±14.74mm;male: 82.95±5.40mm), abdomen width (female: 12.09±1.90mm;male: 11.09±0.88mm), and metasoma length (female: 43.09±3.08mm;male: 44.63±6.50mm) were not significantly different between sexes.
Kovařík František - One of the best experts on this subject based on the ideXlab platform.
-
A new species of \u3cem\u3eAndroctonus\u3c/em\u3e Ehrenberg, 1828 from northwestern Egypt (Scorpiones: Buthidae)
Marshall Digital Scholar, 2016Co-Authors: Teruel Rolando, Kovařík František, Turiel CarlosAbstract:Androctonus tenuissimus sp. n. from two coastal localities placed in northwestern Egypt is herein described, an addition that represents the fifth species of this genus confirmed to occur in this North African country. It is most closely related only to Androctonus bicolor Ehrenberg, 1828, which is widely distributed across northeast Africa and the Middle East and also occurs in Egypt. Both are the only species in the genus whose adults of both sexes show the following combination of three diagnostic characters: coloration uniformly blackish, pedipalp chelae con-spicuously narrower than patella in adults, and pedipalp fingers with basal lobe/notch combination entirely absent. However, these two taxa can readily be distinguished by very marked differences in appendage attenuation, body sculpture and counts of principal rows of denticles on pedipalp fingers, among other characters
-
Redescription of \u3cem\u3eAndroctonus bicolor\u3c/em\u3e Ehrenberg, 1828, and description of \u3cem\u3eAndroctonus turieli\u3c/em\u3e sp. n. from Tunisia (Scorpiones: Buthidae)
Marshall Digital Scholar, 2016Co-Authors: Teruel Rolando, Kovařík FrantišekAbstract:We redescribe Androctonus bicolor Ehrenberg, 1828, a scorpion species widely distributed across northeast Africa and the Middle East, on the basis of the study of nine original syntypes and supplementary material from its entire distribution area. In order to stabilize nomenclature, we also designate a lectotype, update its diagnosis according to modern standards, and provide a full illustrated complement to facilitate the recognition of this species as compared to all of its congeners. Also, a new, closely related species from eastern Tunisia is described
-
A review of \u3cem\u3eAndroctonus finitimus\u3c/em\u3e (Pocock, 1897), with description of two new species from Pakistan and India (Scorpiones, Buthidae)
Marshall Digital Scholar, 2016Co-Authors: Kovařík František, Ahmed ZubairAbstract:We describe Androctonus robustus sp. n. and A. cholistanus sp. n. from Pakistan and India and compare them with A. finitimus (Pocock, 1897), whose holotype we have studied. These three species are closely related and form a group that has hitherto been considered one species. They share coloration and are close to each other in geographic range. However, these three species can be reliably distinguished morphologically, primarily based on morphometry of male metasoma, which is widest in A. robustus sp. n. and narrowest in A. cholistanus sp. n
-
Scorpions of Iran (Arachnida, Scorpiones). Part V. Chahar Mahal & Bakhtiyari Province
Marshall Digital Scholar, 2016Co-Authors: Pirali-kheirabadi Khodadad, Kovařík František, Navidpour Shahrokh, Fet Victor, Soleglad, Michael E.Abstract:Ten species of scorpions belonging to three families are reported from the montane Chahar Mahal & Bakhtiyari Province of Iran. Of these, only Razianus zarudnyi (Birula, 1903) was formerly reported for this province, while nine species are reported for the first time: Androctonus crassicauda (Olivier, 1807), Compsobuthus matthiesseni (Birula, 1905), Hottentotta saulcyi (Simon, 1880), Hottentotta zagrosensis Kovařík, 1997, Mesobuthus eupeus phillipsii (Pocock, 1889), Odontobuthus doriae (Thorell, 1876), Orthochirus zagrosensis Kovařík, 2004, Hemi- scorpius lepturus Peters, 1861, and Scorpio maurus townsendi (Pocock, 1900). Also presented is a key to all species of scorpions found in the Chahar Mahal & Bakhtiyari Province
-
Scorpions of Iran (Arachnida, Scorpiones). Part IV. Kohgilouyeh & Boyer Ahmad Province
Marshall Digital Scholar, 2016Co-Authors: Navidpour Shahrokh, Kovařík František, Soleglad, Michael E., Fet VictorAbstract:According to previous surveys, only Mesobuthus eupeus phillipsii (Pocock, 1889), Orthochirus zagrosensis Kovařík, 2004, and Hemiscorpius lepturus Peters, 1861 have been recorded from Kohgilouyeh & Boyer Ahmad Province. Collections made by a team under Shahrokh Navidpour (Razi Reference Laboratory of Scorpion Research, Razi Vaccine and Serum Research Institute, Ahvaz, Khoozestan, Iran) reveal eight other species belonging to two families recorded from the province for the first time: Androctonus crassicauda (Olivier, 1807); Compsobuthus matthiesseni (Birula, 1905); Hottentotta saulcyi (Simon, 1880); Hottentotta zagrosensis Kovařík, 1997; Odontobuthus bidentatus Lourenço et Pézier, 2002; Orthochirus iranus Kovařík, 2004; Razianus zarudnyi (Birula, 1903); and Scorpio maurus townsendi (Pocock, 1900). Also presented is a key to all species of scorpions found in the province