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Lourival D Possani - One of the best experts on this subject based on the ideXlab platform.

  • full neutralization of Centruroides sculpturatus scorpion venom by combining two human antibody fragments
    Toxins, 2021
    Co-Authors: Lidia Rianoumbarila, Lourival D Possani, Timoteo Olamendiportugal, Jose Alberto Romeromoreno, Luis M Ledezmacandanoza, Baltazar Becerril
    Abstract:

    A fundamental issue of the characterization of single-chain variable fragments (scFvs), capable of neutralizing scorpion toxins, is their cross-neutralizing ability. This aspect is very important in Mexico because all scorpions dangerous to humans belong to the Centruroides genus, where toxin sequences show high identity. Among toxin-neutralizing antibodies that were generated in a previous study, scFv 10FG2 showed a broad cross-reactivity against several Centruroides toxins, while the one of scFv LR is more limited. Both neutralizing scFvs recognize independent epitopes of the toxins. In the present work, the neutralization capacity of these two scFvs against two medically important toxins of the venom of Centruroides sculpturatus Ewing was evaluated. The results showed that these toxins are recognized by both scFvs with affinities between 1.8 × 10-9 and 6.1 × 10-11 M. For this reason, their ability to neutralize the venom was evaluated in mice, where scFv 10FG2 showed a better protective capacity. A combination of both scFvs at a molar ratio of 1:5:5 (toxins: scFv 10FG2: scFv LR) neutralized the venom without the appearance of any signs of intoxication. These results indicate a complementary activity of these two scFvs during venom neutralization.

  • the three dimensional structure of the toxic peptide cl13 from the scorpion Centruroides limpidus
    Toxicon, 2020
    Co-Authors: Andrea Estefania Lopezgiraldo, Lourival D Possani, Timoteo Olamendiportugal, Lidia Rianoumbarila, Baltazar Becerril, Muriel Delepierre, Federico Del Rioportilla
    Abstract:

    Cl13 is a toxin purified previously from the venom of the Mexican scorpion Centruroides limpidus. This toxin affects the function of voltage gated Na+-channels, human subtypes Nav1.4, Nav1.5 and Nav1.6 in a similar manner as other known β-toxins from scorpion venoms. Here, we report a correction of the primary structure of Cl13, previously published. The peptide does contain 66 amino acids, but residue 58 is a tryptophan and the last C-terminal amino acid is an amidated lysine, instead of arginine. The main contribution of this communication is the determination of the 3D-structure of Cl13, by solution NMR, showing that Cl13 has the classical cysteine-stabilized α/β (CSα/β) folding. It has a triple stranded antiparallel beta sheet commonly present in scorpion sodium channel β-toxins. In addition, we report and discuss a comparison of Cl13 structure with two other toxins (Cn2 and Css2) from scorpions of the same genus Centruroides, which shows important surface similarities with the structure reported here. Finally, the lack of neutralization of Cl13 toxin by two single-chain antibody fragments (scFvs), named LR and 10FG2, which are capable of neutralizing various toxins from Mexican scorpions, is revised. In particular, 10FG2 is capable of neutralizing toxins Cll1 and Cll2 of the same scorpion C. limpidus. The reasons why LR and 10FG2 are unable of neutralizing Cl13 toxin are discussed.

  • biochemical characterization of the venom from the mexican scorpion Centruroides ornatus a dangerous species to humans
    Toxicon, 2020
    Co-Authors: I A Garciaguerrero, Fernando Z Zamudio, Georgina B Gurrola, Edson Norberto Carcamonoriega, Froylan Gomezlagunas, Edmundo Gonzalezsantillan, Lourival D Possani
    Abstract:

    Abstract Every year in Mexico, around 300,000 people suffer from accidents related to scorpion stings. Among the scorpion species dangerous to human is Centruroides ornatus, whose venom characterization is described here. From this venom, a total of 114 components were found using chromatographic separation and mass spectrometry analysis. The most abundant ones have molecular masses between 3000-4000 Da and 6000–8000 Da respectively, similar to other known K+ and Na+-channel specific scorpion peptides. Using intraperitoneal injections into CD1 mice, we were able to identify and fully sequenced three new lethal toxins. We propose to name them Co1, Co2 and Co3 toxins, which correspond to toxins 1 to 3 of the abbreviated species name (Co). Electrophysiology analysis of these peptides using heterologously expressed human Na+-channels revealed a typical β-toxin effect. Peptide Co52 (the most abundant peptide in the venom) showed no activity in our in vivo and in vitro model assays. A phylogenetic analysis groups the Co1, Co2 and Co3 among other β-toxins from Centruroides scorpions. Peptide Co52 segregates among peptides of unknown defined functions.

  • Dissecting Toxicity: The Venom Gland Transcriptome and the Venom Proteome of the Highly Venomous Scorpion Centruroides limpidus (Karsch, 1879)
    MDPI AG, 2019
    Co-Authors: Jimena I. Cid-uribe, Erika P. Meneses, Cesar V. F. Batista, Ernesto Ortiz, Lourival D Possani
    Abstract:

    Venom glands and soluble venom from the Mexican scorpion Centruroides limpidus (Karsch, 1879) were used for transcriptomic and proteomic analyses, respectively. An RNA-seq was performed by high-throughput sequencing with the Illumina platform. Approximately 80 million reads were obtained and assembled into 198,662 putative transcripts, of which 11,058 were annotated by similarity to sequences from available databases. A total of 192 venom-related sequences were identified, including Na+ and K+ channel-acting toxins, enzymes, host defense peptides, and other venom components. The most diverse transcripts were those potentially coding for ion channel-acting toxins, mainly those active on Na+ channels (NaScTx). Sequences corresponding to β- scorpion toxins active of K+ channels (KScTx) and λ-KScTx are here reported for the first time for a scorpion of the genus Centruroides. Mass fingerprint corroborated that NaScTx are the most abundant components in this venom. Liquid chromatography coupled to mass spectometry (LC-MS/MS) allowed the identification of 46 peptides matching sequences encoded in the transcriptome, confirming their expression in the venom. This study corroborates that, in the venom of toxic buthid scorpions, the more abundant and diverse components are ion channel-acting toxins, mainly NaScTx, while they lack the HDP diversity previously demonstrated for the non-buthid scorpions. The highly abundant and diverse antareases explain the pancreatitis observed after envenomation by this species

  • Venom content and toxicity regeneration after venom gland depletion by electrostimulation in the scorpion Centruroides limpidus.
    Toxicon, 2019
    Co-Authors: Edson Norberto Carcamo-noriega, Lourival D Possani, Ernesto Ortiz
    Abstract:

    Abstract The scorpion venom is a cocktail of many components. Its composition can exhibit a level of plasticity in response to different behavioral and environmental factors, leading to intraspecific variation. The toxicity and specificity of scorpion venoms appear to be taxon-dependent, due to a co-evolutionary interaction with prey and predators, which shaped the composition at the molecular level. The venom regeneration by the venom glands is an asynchronous process, in which particular components are expressed at different stages and at different rates. According to this, it can be reasonably assumed that the regeneration of toxicity in the venom is also asynchronous. In this work, we studied the toxicity regeneration dynamics by the scorpion Centruroides limpidus after full venom depletion by electrical stimulation. For this, we evaluated the toxicity of venom samples extracted at different days post depletion, against insects (crickets) and mammals (humans, by assessing the venom activity on the human voltage-dependent Na+ channel Nav1.6). The regeneration of toxicity against humans lagged behind that against crickets (13 vs 10 days, respectively). Thirteen days after depletion the venom seems to be replenished. Our results show asynchrony in the regeneration of species-specific toxic activity in the venom of Centruroides limpidus. The understanding of the venom regeneration kinetics for the different scorpion species will help to design venom extraction protocols that could maximize the yield and quality of the collected venoms.

Baltazar Becerril - One of the best experts on this subject based on the ideXlab platform.

  • full neutralization of Centruroides sculpturatus scorpion venom by combining two human antibody fragments
    Toxins, 2021
    Co-Authors: Lidia Rianoumbarila, Lourival D Possani, Timoteo Olamendiportugal, Jose Alberto Romeromoreno, Luis M Ledezmacandanoza, Baltazar Becerril
    Abstract:

    A fundamental issue of the characterization of single-chain variable fragments (scFvs), capable of neutralizing scorpion toxins, is their cross-neutralizing ability. This aspect is very important in Mexico because all scorpions dangerous to humans belong to the Centruroides genus, where toxin sequences show high identity. Among toxin-neutralizing antibodies that were generated in a previous study, scFv 10FG2 showed a broad cross-reactivity against several Centruroides toxins, while the one of scFv LR is more limited. Both neutralizing scFvs recognize independent epitopes of the toxins. In the present work, the neutralization capacity of these two scFvs against two medically important toxins of the venom of Centruroides sculpturatus Ewing was evaluated. The results showed that these toxins are recognized by both scFvs with affinities between 1.8 × 10-9 and 6.1 × 10-11 M. For this reason, their ability to neutralize the venom was evaluated in mice, where scFv 10FG2 showed a better protective capacity. A combination of both scFvs at a molar ratio of 1:5:5 (toxins: scFv 10FG2: scFv LR) neutralized the venom without the appearance of any signs of intoxication. These results indicate a complementary activity of these two scFvs during venom neutralization.

  • the venom of the scorpion Centruroides limpidus which causes the highest number of stings in mexico is neutralized by two recombinant antibody fragments
    Molecular Immunology, 2021
    Co-Authors: Guillermo Fernandeztaboada, Lidia Rianoumbarila, Ilse V Gomezramirez, Alejandro Olverarodriguez, Luis Fernando Losoyauribe, Baltazar Becerril
    Abstract:

    Phage display and directed evolution have made it possible to generate recombinant antibodies in the format of single chain variable fragments (scFvs) capable of neutralizing different toxins and venoms of Mexican scorpions. Despite having managed to neutralize a significant number of venoms, some others have not yet been completely neutralized, due to the diversity of the toxic components present in them. An example is the venom of the scorpion Centruroides limpidus, which contains three toxins of medical importance, called Cll1, Cll2 and Cl13. The first two are neutralized by scFv 10FG2, while Cl13, due to its sequence divergence, was not even recognized. For this reason, the aim of the present work was the generation of a new scFv capable of neutralizing Cl13 toxin and thereby helping to neutralize the whole venom of this scorpion. By hybridoma technology, a monoclonal antibody (mAb B7) was generated, which was able to recognize and partially neutralize Cl13 toxin. From mAb B7, its scFv format was obtained, named scFv B7 and subjected to three cycles of directed evolution. At the end of these processes, scFv 11F which neutralized Cl13 toxin was obtained. This scFv, administered in conjunction with scFv 10FG2, allowed to fully neutralize the whole venom of Centruroides limpidus scorpion.

  • the three dimensional structure of the toxic peptide cl13 from the scorpion Centruroides limpidus
    Toxicon, 2020
    Co-Authors: Andrea Estefania Lopezgiraldo, Lourival D Possani, Timoteo Olamendiportugal, Lidia Rianoumbarila, Baltazar Becerril, Muriel Delepierre, Federico Del Rioportilla
    Abstract:

    Cl13 is a toxin purified previously from the venom of the Mexican scorpion Centruroides limpidus. This toxin affects the function of voltage gated Na+-channels, human subtypes Nav1.4, Nav1.5 and Nav1.6 in a similar manner as other known β-toxins from scorpion venoms. Here, we report a correction of the primary structure of Cl13, previously published. The peptide does contain 66 amino acids, but residue 58 is a tryptophan and the last C-terminal amino acid is an amidated lysine, instead of arginine. The main contribution of this communication is the determination of the 3D-structure of Cl13, by solution NMR, showing that Cl13 has the classical cysteine-stabilized α/β (CSα/β) folding. It has a triple stranded antiparallel beta sheet commonly present in scorpion sodium channel β-toxins. In addition, we report and discuss a comparison of Cl13 structure with two other toxins (Cn2 and Css2) from scorpions of the same genus Centruroides, which shows important surface similarities with the structure reported here. Finally, the lack of neutralization of Cl13 toxin by two single-chain antibody fragments (scFvs), named LR and 10FG2, which are capable of neutralizing various toxins from Mexican scorpions, is revised. In particular, 10FG2 is capable of neutralizing toxins Cll1 and Cll2 of the same scorpion C. limpidus. The reasons why LR and 10FG2 are unable of neutralizing Cl13 toxin are discussed.

  • intraspecific variation of Centruroides sculpturatus scorpion venom from two regions of arizona
    Archives of Biochemistry and Biophysics, 2018
    Co-Authors: Edson Norberto Carcamonoriega, Ashlee H Rowe, Timoteo Olamendiportugal, Baltazar Becerril, Rita Restanocassulini, Selene Jocelyn Uriberomero, Lourival D Possani
    Abstract:

    Abstract This study investigated geographic variability in the venom of Centruroides sculpturatus scorpions from different biotopes. Venom from scorpions collected from two different regions in Arizona; Santa Rita Foothills (SR) and Yarnell (Yar) were analyzed. We found differences between venoms, mainly in the two most abundant peptides; SR (CsEv2e and CsEv1f) and Yar (CsEv2 and CsEv1c) identified as natural variants of CsEv1 and CsEv2. Sequence analyses of these peptides revealed conservative amino acid changes between variants, which may underlie biological activity against arthropods. A third peptide (CsEv6) was highly abundant in the Yar venom compared to the SR venom. CsEv6 is a 67 amino acid peptide with 8 cysteines. CsEv6 did not exhibit toxicity to the three animal models tested. However, both venoms shared similarities in peptides that are predicted to deter predators. For example, both venoms expressed CsEI (lethal to chick) in similar abundance, while CsEd and CsEM1a (toxic to mammals) displayed only moderate variation in their abundance. Electrophysiological evaluation of CsEd and CsEM1a showed that both toxins act on the human sodium-channel subtype 1.6 (hNav 1.6). Complete sequencing revealed that both toxins are structurally similar to beta-toxins isolated from different Centruroides species that also target hNav 1.6.

  • broadening the neutralizing capacity of a family of antibody fragments against different toxins from mexican scorpions
    Toxicon, 2016
    Co-Authors: Everardo Remi Rodriguezrodriguez, Lourival D Possani, Timoteo Olamendiportugal, Lidia Rianoumbarila, Hugo Serranoposada, Jonathan Noe Arredondolopez, Ilse V Gomezramirez, Guillermo Fernandeztaboada, Gerardo Alfonso Anguianovega, Baltazar Becerril
    Abstract:

    New approaches aimed at neutralizing the primary toxic components present in scorpion venoms, represent a promising alternative to the use of antivenoms of equine origin in humans. New potential therapeutics developed by these approaches correspond to neutralizing antibody fragments obtained by selection and maturation processes from libraries of human origin. The high sequence identity shared among scorpion toxins is associated with an important level of cross reactivity exhibited by these antibody fragments. We have exploited the cross reactivity showed by single chain variable antibody fragments (scFvs) of human origin to re-direct the neutralizing capacity toward various other scorpion toxins. As expected, during these evolving processes several variants derived from a parental scFv exhibited the capacity to simultaneously recognize and neutralize different toxins from Centruroides scorpion venoms. A sequence analyses of the cross reacting scFvs revealed that specific mutations are responsible for broadening their neutralizing capacity. In this work, we generated a set of new scFvs that resulted from the combinatorial insertion of these point mutations. These scFvs are potential candidates to be part of a novel recombinant antivenom of human origin that could confer protection against scorpion stings. A remarkable property of one of these new scFvs (ER-5) is its capacity to neutralize at least three different toxins and its complementary capacity to neutralize the whole venom from Centruroides suffusus in combination with a second scFv (LR), which binds to a different epitope shared by Centruroides scorpion toxins.

Lidia Rianoumbarila - One of the best experts on this subject based on the ideXlab platform.

  • full neutralization of Centruroides sculpturatus scorpion venom by combining two human antibody fragments
    Toxins, 2021
    Co-Authors: Lidia Rianoumbarila, Lourival D Possani, Timoteo Olamendiportugal, Jose Alberto Romeromoreno, Luis M Ledezmacandanoza, Baltazar Becerril
    Abstract:

    A fundamental issue of the characterization of single-chain variable fragments (scFvs), capable of neutralizing scorpion toxins, is their cross-neutralizing ability. This aspect is very important in Mexico because all scorpions dangerous to humans belong to the Centruroides genus, where toxin sequences show high identity. Among toxin-neutralizing antibodies that were generated in a previous study, scFv 10FG2 showed a broad cross-reactivity against several Centruroides toxins, while the one of scFv LR is more limited. Both neutralizing scFvs recognize independent epitopes of the toxins. In the present work, the neutralization capacity of these two scFvs against two medically important toxins of the venom of Centruroides sculpturatus Ewing was evaluated. The results showed that these toxins are recognized by both scFvs with affinities between 1.8 × 10-9 and 6.1 × 10-11 M. For this reason, their ability to neutralize the venom was evaluated in mice, where scFv 10FG2 showed a better protective capacity. A combination of both scFvs at a molar ratio of 1:5:5 (toxins: scFv 10FG2: scFv LR) neutralized the venom without the appearance of any signs of intoxication. These results indicate a complementary activity of these two scFvs during venom neutralization.

  • the venom of the scorpion Centruroides limpidus which causes the highest number of stings in mexico is neutralized by two recombinant antibody fragments
    Molecular Immunology, 2021
    Co-Authors: Guillermo Fernandeztaboada, Lidia Rianoumbarila, Ilse V Gomezramirez, Alejandro Olverarodriguez, Luis Fernando Losoyauribe, Baltazar Becerril
    Abstract:

    Phage display and directed evolution have made it possible to generate recombinant antibodies in the format of single chain variable fragments (scFvs) capable of neutralizing different toxins and venoms of Mexican scorpions. Despite having managed to neutralize a significant number of venoms, some others have not yet been completely neutralized, due to the diversity of the toxic components present in them. An example is the venom of the scorpion Centruroides limpidus, which contains three toxins of medical importance, called Cll1, Cll2 and Cl13. The first two are neutralized by scFv 10FG2, while Cl13, due to its sequence divergence, was not even recognized. For this reason, the aim of the present work was the generation of a new scFv capable of neutralizing Cl13 toxin and thereby helping to neutralize the whole venom of this scorpion. By hybridoma technology, a monoclonal antibody (mAb B7) was generated, which was able to recognize and partially neutralize Cl13 toxin. From mAb B7, its scFv format was obtained, named scFv B7 and subjected to three cycles of directed evolution. At the end of these processes, scFv 11F which neutralized Cl13 toxin was obtained. This scFv, administered in conjunction with scFv 10FG2, allowed to fully neutralize the whole venom of Centruroides limpidus scorpion.

  • the three dimensional structure of the toxic peptide cl13 from the scorpion Centruroides limpidus
    Toxicon, 2020
    Co-Authors: Andrea Estefania Lopezgiraldo, Lourival D Possani, Timoteo Olamendiportugal, Lidia Rianoumbarila, Baltazar Becerril, Muriel Delepierre, Federico Del Rioportilla
    Abstract:

    Cl13 is a toxin purified previously from the venom of the Mexican scorpion Centruroides limpidus. This toxin affects the function of voltage gated Na+-channels, human subtypes Nav1.4, Nav1.5 and Nav1.6 in a similar manner as other known β-toxins from scorpion venoms. Here, we report a correction of the primary structure of Cl13, previously published. The peptide does contain 66 amino acids, but residue 58 is a tryptophan and the last C-terminal amino acid is an amidated lysine, instead of arginine. The main contribution of this communication is the determination of the 3D-structure of Cl13, by solution NMR, showing that Cl13 has the classical cysteine-stabilized α/β (CSα/β) folding. It has a triple stranded antiparallel beta sheet commonly present in scorpion sodium channel β-toxins. In addition, we report and discuss a comparison of Cl13 structure with two other toxins (Cn2 and Css2) from scorpions of the same genus Centruroides, which shows important surface similarities with the structure reported here. Finally, the lack of neutralization of Cl13 toxin by two single-chain antibody fragments (scFvs), named LR and 10FG2, which are capable of neutralizing various toxins from Mexican scorpions, is revised. In particular, 10FG2 is capable of neutralizing toxins Cll1 and Cll2 of the same scorpion C. limpidus. The reasons why LR and 10FG2 are unable of neutralizing Cl13 toxin are discussed.

  • broadening the neutralizing capacity of a family of antibody fragments against different toxins from mexican scorpions
    Toxicon, 2016
    Co-Authors: Everardo Remi Rodriguezrodriguez, Lourival D Possani, Timoteo Olamendiportugal, Lidia Rianoumbarila, Hugo Serranoposada, Jonathan Noe Arredondolopez, Ilse V Gomezramirez, Guillermo Fernandeztaboada, Gerardo Alfonso Anguianovega, Baltazar Becerril
    Abstract:

    New approaches aimed at neutralizing the primary toxic components present in scorpion venoms, represent a promising alternative to the use of antivenoms of equine origin in humans. New potential therapeutics developed by these approaches correspond to neutralizing antibody fragments obtained by selection and maturation processes from libraries of human origin. The high sequence identity shared among scorpion toxins is associated with an important level of cross reactivity exhibited by these antibody fragments. We have exploited the cross reactivity showed by single chain variable antibody fragments (scFvs) of human origin to re-direct the neutralizing capacity toward various other scorpion toxins. As expected, during these evolving processes several variants derived from a parental scFv exhibited the capacity to simultaneously recognize and neutralize different toxins from Centruroides scorpion venoms. A sequence analyses of the cross reacting scFvs revealed that specific mutations are responsible for broadening their neutralizing capacity. In this work, we generated a set of new scFvs that resulted from the combinatorial insertion of these point mutations. These scFvs are potential candidates to be part of a novel recombinant antivenom of human origin that could confer protection against scorpion stings. A remarkable property of one of these new scFvs (ER-5) is its capacity to neutralize at least three different toxins and its complementary capacity to neutralize the whole venom from Centruroides suffusus in combination with a second scFv (LR), which binds to a different epitope shared by Centruroides scorpion toxins.

  • structural basis of neutralization of the major toxic component from the scorpion Centruroides noxius hoffmann by a human derived single chain antibody fragment
    Journal of Biological Chemistry, 2011
    Co-Authors: Juan Carlos Canultec, Lourival D Possani, Lidia Rianoumbarila, Baltazar Becerril, Enrique Rudinopinera, Alfredo Torreslarios
    Abstract:

    It has previously been reported that several single-chain antibody fragments of human origin (scFv) neutralize the effects of two different scorpion venoms through interactions with the primary toxins of Centruroides noxius Hoffmann (Cn2) and Centruroides suffusus suffusus (Css2). Here we present the crystal structure of the complex formed between one scFv (9004G) and the Cn2 toxin, determined in two crystal forms at 2.5 and 1.9 Å resolution. A 15-residue span of the toxin is recognized by the antibody through a cleft formed by residues from five of the complementarity-determining regions of the scFv. Analysis of the interface of the complex reveals three features. First, the epitope of toxin Cn2 overlaps with essential residues for the binding of β-toxins to its Na+ channel receptor site. Second, the putative recognition of Css2 involves mainly residues that are present in both Cn2 and Css2 toxins. Finally, the effect on the increase of affinity of previously reported key residues during the maturation process of different scFvs can be inferred from the structure. Taken together, these results provide the structural basis that explain the mechanism of the 9004G neutralizing activity and give insight into the process of directed evolution that gave rise to this family of neutralizing scFvs.

De Armas, Luis F - One of the best experts on this subject based on the ideXlab platform.

  • Identity of the Central American scorpion \u3cem\u3eCentruroides mahnerti\u3c/em\u3e Lourenço, 1983 (Scorpiones: Buthidae)
    Marshall Digital Scholar, 2019
    Co-Authors: De Armas, Luis F
    Abstract:

    The Central American scorpion Centruroides mahnerti Lourenço, 1983, was described on the basis of three female specimens (holotype and paratypes) from Momotombo Volcano, Nicaragua. Almost two decades later, it was synonymized under Centruroides koesteri Kraepelin, 1911 by Armas and Maes, without examination of the type specimen; but Teruel and Stockwell posteriorly argued that description and figures given for C. mahnerti are also similarly referable to juveniles of C. edwardsii (Gervais, 1843). Now, an evaluation of the holotype of C. mahnerti has definitively shown that it is a subadult female of C. koesteri. For the first time, photographs of the holotype of C. mahnerti are presented

  • A new species of \u3cem\u3eMicrotityus\u3c/em\u3e from the British Virgin Islands, West Indies, and new localities for other scorpions (Scorpiones: Buthidae, Scorpionidae)
    Marshall Digital Scholar, 2018
    Co-Authors: De Armas, Luis F
    Abstract:

    Microtityus (Parvabsonus) eustatia sp. n. is herein described from the British Virgin Islands (West Indies): Eustatia Island (type locality), Virgin Gorda Island, and Camanoe Island, based on seven specimens (three males and four females). The new species closely resembles M. waeringi Francke & Sissom, 1980 from St. John Island and St. Thomas Island, U.S. Virgin Islands, differing mainly by the fixed finger of pedipalp having ten rows of denticles (nine in M. waeringi) and more attenuated metasoma. Also, new localities are recorded for Heteronebo yntemai Francke & Sissom, 1980 (Scorpionidae) and Centruroides griseus (C. L. Koch, 1844) (Buthidae)

  • First record of \u3cem\u3eCentruroides alayoni\u3c/em\u3e Armas, 1999 (Scorpiones: Buthidae) from Haiti, Greater Antilles
    Marshall Digital Scholar, 2017
    Co-Authors: De Armas, Luis F
    Abstract:

    Centruroides haitiensis Lourenço, 2016, from Grande Cayemite, Haiti, is regarded as a junior synonym of Centruroides alayoni Armas, 1999, previously known from southern Pedernales Province (215 km east of Grande Cayemite), Dominican Republic. Consequently, C. alayoni is herein recorded for the first time from Haiti. The list of the Haitian species of the genus Centruroides Marx, 1890 is given

  • \u3cem\u3eCentruroides thorellii\u3c/em\u3e (Scorpiones: Buthidae): traveling from Guatemala to England without a passport
    Marshall Digital Scholar, 2017
    Co-Authors: Trujillo, Rony E., De Armas, Luis F, Mansfield Darren
    Abstract:

    We recorded a pregnant female of the Central American bark stripped scorpion Centruroides thorellii (Kraepelin, 1891), which arrived to England as a stowaway in the bag of a woman that previously visited the Departments of Sacatepéquez, Sololá and San Marcos, Guatemala. On January 2, this C. thorellii female had a litter of three off-spring and three infertile eggs, but she has eaten them, probably as consequence of the stress caused by the hard travel and the environmental changes. We provide a map with the geographical distribution of this species and photos of the female detected in a British train

  • Escorpiones (Arachnida) del Archipiélago de Bocas del Toro, Panamá
    'Universidad de Costa Rica', 2016
    Co-Authors: Montoya Michel, De Armas, Luis F
    Abstract:

    Four species of buthid scorpions (Ananteris platnicki Lourenço, 1993; Centruroides limbatus [Pocock, 1898]; Tityus pachyurus [Pocock, 1897]; and T. ocelote Francke and Stockwell, 1987) are recorded for the first time from some islands and cays of the Bocas del Toro Archipelago, Panama. Morphological variation and ecological data are given for all the species. This is the first Panamanian record for both C. limbatus and T. ocelote. The scorpion fauna of the Bocas de Toro Archipelago is related with the recent fauna of the Atlantic continental lowland region of Costa Rica and Panama and includes Amazonian-Guyanese (genera Ananteris and Tityus) as well as Mexican-North Central American (genus Centruroides) elementsSe registran por primera vez cuatro especies de escorpiones de la familia Buthidae (Ananteris platnicki Lourenço, 1993, Centruroides limbatus [Pocock, 1898], Tityus pachyurus [Pocock, 1897] y T. ocelote Francke y Stockwell, 1987) en islas y cayos del Archipiélago de Bocas del Toro, Panamá. Para cada especie se ofrece información sobre variación morfológica y ecología. Este es el primer registro para Panamá de C. limbatus y T. ocelote. La fauna de escorpiones del Archipiélago de Bocas del Toro está relacionada con la fauna de las zonas bajas de la vertiente caribeña de Costa Rica y Panamá y contiene elementos Amazónico- Guyaneses (géneros Ananteris y Tityus) y Mexicanos- Norte Centroamericanos (género Centruroides)

Matthew P Rowe - One of the best experts on this subject based on the ideXlab platform.

  • physiological resistance of grasshopper mice onychomys spp to arizona bark scorpion Centruroides exilicauda venom
    Toxicon, 2008
    Co-Authors: Ashlee H Rowe, Matthew P Rowe
    Abstract:

    Abstract Predators feeding on toxic prey may evolve physiological resistance to the preys' toxins. Grasshopper mice ( Onychomys spp.) are voracious predators of scorpions in North American deserts. Two species of grasshopper mice ( Onychomys torridus and Onychomys arenicola ) are broadly sympatric with two species of potentially lethal bark scorpion ( Centruroides exilicauda and Centruroides vittatus ) in the Sonoran and Chihuahuan deserts, respectively. Bark scorpions produce toxins that selectively bind sodium (Na + ) and potassium (K + ) ion channels in vertebrate nerve and muscle tissue. We previously reported that grasshopper mice showed no effects of bark scorpion envenomation following natural stings. Here we conducted a series of toxicity tests to determine whether grasshopper mice have evolved resistance to bark scorpion neurotoxins. Five populations of grasshopper mice, either sympatric with or allopatric to bark scorpions, were injected with bark scorpion venom; LD 50 s were estimated for each population. All five populations of grasshopper mice demonstrated levels of venom resistance greater than that reported for non-resistant Mus musculus . Moreover, venom resistance in the mice showed intra- and interspecific variability that covaried with bark scorpion sympatry and allopatry, patterns consistent with the hypothesis that venom resistance in grasshopper mice is an adaptive response to feeding on their neurotoxic prey.

  • risk assessment by grasshopper mice onychomys spp feeding on neurotoxic prey Centruroides spp
    Animal Behaviour, 2006
    Co-Authors: Ashlee H Rowe, Matthew P Rowe
    Abstract:

    Predators should benefit from assessing the risks posed by prey that differ in their dangerousness. Assessment might come at any phase of the predatory sequence: search/recognition, pursuit/attack and handling/subjugation. Grasshopper mice are voracious carnivores in North American deserts, feeding almost exclusively on arthropods. In certain regions, grasshopper mice co-occur with extremely neurotoxic bark scorpions, whose sting can prove lethal to vertebrates. We presented three different prey items to wild-caught grasshopper mice at several field sites in the southwestern U.S. The three items, listed in increasing order of dangerousness, were: laboratory crickets, Acheta domesticus, having few or no defences; two sister species of Vaejovis spp., a non-neurotoxic genus of scorpion; and two sister species of toxic Centruroides. Grasshopper mice made no distinctions among the prey in either the recognition or pursuit phases of the encounter, attacking crickets and both genera of scorpions with little hesitation. There were, however, significant differences in how the mice handled the three different prey types, with Centruroides requiring significantly more effort to subdue. The difficulties that mice had in dispatching Centruroides were not related to the neurotoxic components of these scorpions' venoms, to which the mice are resistant. Instead, the difficulties appeared to result from other constituents of Centruroides' venom that cause intense, short-term pain.