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Lourival D. Possani - One of the best experts on this subject based on the ideXlab platform.
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Head-to-Tail Cyclization after Interaction with Trypsin: A Scorpion Venom Peptide that Resembles Plant Cyclotides.
Journal of Medicinal Chemistry, 2020Co-Authors: Caroline B. F. Mourão, Guilherme D. Brand, João Paulo Campos Fernandes, Maura V. Prates, Carlos Bloch, João Alexandre Ribeiro Gonçalves Barbosa, Sonia Maria De Freitas, Rita Restano-cassulini, Lourival D. Possani, Elisabeth F SchwartzAbstract:Peptidase inhibitors (PIs) have been broadly studied due to their wide therapeutic potential for human diseases. A potent trypsin inhibitor from Tityus obscurus scorpion venom was characterized and...
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identification and phylogenetic analysis of Tityus pachyurus and Tityus obscurus novel putative na channel scorpion toxins
PLOS ONE, 2012Co-Authors: Jimmy Alexander Guerrerovargas, Lourival D. Possani, Caroline B. F. Mourão, Veronica Quinterohernandez, Elisabeth F SchwartzAbstract:Background: Colombia and Brazil are affected by severe cases of scorpionism. In Colombia the most dangerous accidents are caused by Tityus pachyurus that is widely distributed around this country. In the Brazilian Amazonian region scorpion stings are a common event caused by Tityus obscurus. The main objective of this work was to perform the molecular cloning of the putative Na+-channel scorpion toxins (NaScTxs) from T. pachyurus and T. obscurus venom glands and to analyze their phylogenetic relationship with other known NaScTxs from Tityus species. Methodology/Principal Findings: cDNA libraries from venom glands of these two species were constructed and five nucleotide sequences from T. pachyurus were identified as putative modulators of Na+-channels, and were named Tpa4, Tpa5, Tpa6, Tpa7 and Tpa8; the latter being the first anti-insect excitatory b-class NaScTx in Tityus scorpion venom to be described. Fifteen sequences from T. obscurus were identified as putative NaScTxs, among which three had been previously described, and the others were named To4 to To15. The peptides Tpa4, Tpa5, Tpa6, To6, To7, To9, To10 and To14 are closely related to the a-class NaScTxs, whereas Tpa7, Tpa8, To4, To8, To12 and To15 sequences are more related to the b-class NaScTxs. To5 is possibly an arthropod specific toxin. To11 and To13 share sequence similarities with both a and b NaScTxs. By means of phylogenetic analysis using the Maximum Parsimony method and the known NaScTxs from Tityus species, these toxins were clustered into 14 distinct groups. Conclusions/Significance: This communication describes new putative NaScTxs from T. pachyurus and T. obscurus and their phylogenetic analysis. The results indicate clear geographic separation between scorpions of Tityus genus inhabiting the Amazonian and Mountain Andes regions and those distributed over the Southern of the Amazonian rainforest. Based on the consensus sequences for the different clusters, a new nomenclature for the NaScTxs is proposed.
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isolation and characterization of a human antibody fragment specific for ts1 toxin from Tityus serrulatus scorpion
Immunology Letters, 2011Co-Authors: Itzel Amaro, Baltazar Becerril, Lidia Rianoumbarila, Lourival D. PossaniAbstract:Scorpion stings are a common event that occurs in tropical and subtropical areas of the world, being a public health problem in certain countries. In most places, medical treatment relays on antivenoms obtained from the sera of hyper-immunized horses, however some efforts are being made to prepare specific antibodies of human origin, using phage display methodology. This communication describes the strategy followed for obtaining a protective human single chain antibody (scFv) capable of partially neutralizing the effect of Ts1, the major toxin isolated from the venom of the Brazilian scorpion Tityus serrulatus. Phage display technique allowed the isolation of scFv 15e from a human library of antibodies, after four rounds of selection against Ts1. This clone codes for 124 amino acids belonging to the family VH6 and 114 amino acids of family VK4. This scFv also recognizes toxins from the scorpions Tityus packyurus and Tityus cambridgei from the Amazonian region. Mice challenged with a LD(50) of Ts1 in the presence of this scFv were substantially resistant to intoxication. ScFv 15e is a leading compound for the development of better anti-scorpion antidotes.
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macrophage activation phagocytosis and intracellular calcium oscillations induced by scorpion toxins from Tityus serrulatus
Clinical and Experimental Immunology, 2008Co-Authors: Vera L Petricevich, Enrique Reynaud, Anselmo Hernandez Cruz, Lourival D. PossaniAbstract:The research described here is focused upon studying the activation of mice peritoneal macrophages when submitted to in vitro effects of Tityus serrulatus scorpion venom and its major toxic peptides. Several functional events were analysed, such as: cytotoxicity, spreading, extent of phagocytosis, vacuole formation and changes of internal calcium concentration. Among the main results observed, when macrophages are subjected to the effects of soluble venom of Tityus serrulatus scorpion venom, a partially purified fraction (FII) or a pure toxin (Ts1), are an increment in the percentage of phagocytosis and vacuole formation, a decrement of the spreading ability, accompanied by oscillations of internal calcium concentration. The net results demonstrate that scorpion venom or its major toxins are effective stimulators of macrophage activity; the effect of whole soluble venom or partially purified fractions is due to the toxic peptides, seen here clearly with Ts1. The possible involvement of Na+-channels in these events is discussed. A basic understanding of the underlying molecular mechanisms responsible for macrophage activation should serve as a foundation for novel drug development aimed at modulating macrophage activity.
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the brazilian scorpion Tityus costatus karsch genes peptides and function
Toxicon, 2005Co-Authors: Elia Diegogarcia, Denise Maria Candido, Sylvia M Lucas, Cesar Vicente Ferreira Batista, Blanca I Garciagomez, Froylan Gomezlagunas, Lourival D. PossaniAbstract:The venom of the scorpion Tityus costatus contains peptides toxic to humans but scarce information on their structure and function is available. Here, we report the separation of 50 different components by high performance liquid chromatography and the identification of approximately 90 distinct components by mass spectrometry analysis, with molecular weights varying from 413 to 45482 atomic mass units. Four peptides were fully sequenced: (i) a butantoxin-like peptide that blocks Shaker K+ channel; (ii) an insect toxin-like peptide; (iii) a scorpine-like peptide, and a short heptapeptide of unknown function. Fifteen peptides were directly sequenced at the N-terminal region, among which are components toxic to mice. A cDNA library was constructed and 13 clones were isolated and sequenced. Some of these peptides and genes are similar to other known scorpion toxins. Based on these results, stings by scorpions of the species Tityus costatus should be taken with caution by medical doctors.
Baltazar Becerril - One of the best experts on this subject based on the ideXlab platform.
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isolation and characterization of a human antibody fragment specific for ts1 toxin from Tityus serrulatus scorpion
Immunology Letters, 2011Co-Authors: Itzel Amaro, Baltazar Becerril, Lidia Rianoumbarila, Lourival D. PossaniAbstract:Scorpion stings are a common event that occurs in tropical and subtropical areas of the world, being a public health problem in certain countries. In most places, medical treatment relays on antivenoms obtained from the sera of hyper-immunized horses, however some efforts are being made to prepare specific antibodies of human origin, using phage display methodology. This communication describes the strategy followed for obtaining a protective human single chain antibody (scFv) capable of partially neutralizing the effect of Ts1, the major toxin isolated from the venom of the Brazilian scorpion Tityus serrulatus. Phage display technique allowed the isolation of scFv 15e from a human library of antibodies, after four rounds of selection against Ts1. This clone codes for 124 amino acids belonging to the family VH6 and 114 amino acids of family VK4. This scFv also recognizes toxins from the scorpions Tityus packyurus and Tityus cambridgei from the Amazonian region. Mice challenged with a LD(50) of Ts1 in the presence of this scFv were substantially resistant to intoxication. ScFv 15e is a leading compound for the development of better anti-scorpion antidotes.
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toxins and genes isolated from scorpions of the genus Tityus
Toxicon, 1997Co-Authors: Baltazar Becerril, Sergio MarangoniAbstract:Scorpion venoms contain a variety of low mol. wt peptides toxic to different organisms. These peptides have been intensively studied because they represent excellent models for investigating structure-function relationships and they are also fine probes for studying ionic channel functions. This review deals with the biological and chemical aspects of toxic peptides that affect Na1 or K1 channels and the cloning of the cDNAs and genes encoding the main α and β neurotoxins present in the venom of the three most dangerous species of Brazilian scorpion. Tityus bahiensis, Tityus stigmurus and Tityus serrulatus, and the Venezuelan scorpion Tityus discrepans. At least 16 different peptides specific for Na+ channels and five affecting K channels were isolated and characterized from the venom of these scorpions. The isolatio of cDNAs and genes encoding four distinct toxins has permitted the elucidation of their nucleotide sequences as well as their genomic organization. Venoms and isolated toxins from scorpions of the genus Tityus were shown to enhance the secretory activity of the pancreas. Antisera obtained against venom of T. serrulatus show cross-reactivity with other species of the Brazilian scorpions.
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toxic peptides and genes encoding toxin gamma of the brazilian scorpions Tityus bahiensis and Tityus stigmurus
Biochemical Journal, 1996Co-Authors: Baltazar Becerril, Miguel Corona, Fredy I V Coronas, Fernando Z Zamudio, Emma S Calderonaranda, Paul L Fletcher, Brian M Martin, Lourival D. PossaniAbstract:Seven toxic peptides from the venom of Tityus bahiensis and Tityus stigmurus was isolated and sequenced, five of them to completion. The most abundant peptide from each of these two species of scorpion was 95% identical with that of toxin gamma from the venom of Tityus serrulatus. They were consequently named gamma-b and gamma-st respectively. The genes encoding these new gamma-like peptides were cloned and sequenced by utilizing oligonucleotides synthesized according to known cDNA sequences of toxin gamma, and amplified by PCR on templates of DNA purified from both T. bahiensis and T. stigmurus. They contain an intron of approx. 470 bp. Possible mechanisms of processing and expressing these peptides are discussed, in view of the fact that glycine is the first residue of the N-terminal sequence of T. stigmurus, whereas lysine is the residue at position 1 of toxin gamma from T. serrulatus and T. bahiensis. In addition, chemical characterization of the less abundant toxic peptides showed the presence of at least four distinct families of peptides in all three species of the genus Tityus studied. There is a large degree of similarity among peptides from different venoms of the same family. By using specific horse and rabbit antisera, the venoms of T. bahiensis, T. serrulatus and T. stigmurus were compared. They showed an extended degree of cross-reactivity. Thus these three species of scorpion have similar toxic components, the genes of which are similarly organized, processed and expressed.
Elisabeth F Schwartz - One of the best experts on this subject based on the ideXlab platform.
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Head-to-Tail Cyclization after Interaction with Trypsin: A Scorpion Venom Peptide that Resembles Plant Cyclotides.
Journal of Medicinal Chemistry, 2020Co-Authors: Caroline B. F. Mourão, Guilherme D. Brand, João Paulo Campos Fernandes, Maura V. Prates, Carlos Bloch, João Alexandre Ribeiro Gonçalves Barbosa, Sonia Maria De Freitas, Rita Restano-cassulini, Lourival D. Possani, Elisabeth F SchwartzAbstract:Peptidase inhibitors (PIs) have been broadly studied due to their wide therapeutic potential for human diseases. A potent trypsin inhibitor from Tityus obscurus scorpion venom was characterized and...
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the scorpion toxin tf2 from Tityus fasciolatus promotes nav1 3 opening
PLOS ONE, 2015Co-Authors: Thalita Soares Camargos, Frank Bosmans, Solange Cristina Rego, Caroline Barbosa Farias Mourao, Elisabeth F SchwartzAbstract:We identified Tf2, the first β-scorpion toxin from the venom of the Brazilian scorpion Tityus fasciolatus. Tf2 is identical to Tb2-II found in Tityus bahiensis. We found that Tf2 selectively activates human (h)Nav1.3, a neuronal voltage-gated sodium (Nav) subtype implicated in epilepsy and nociception. Tf2 shifts hNav1.3 activation voltage to more negative values, thereby opening the channel at resting membrane potentials. Seven other tested mammalian Nav channels (Nav1.1-1.2; Nav1.4-1.8) expressed in Xenopus oocytes are insensitive upon application of 1 μM Tf2. Therefore, the identification of Tf2 represents a unique addition to the repertoire of animal toxins that can be used to investigate Nav channel function.
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identification and phylogenetic analysis of Tityus pachyurus and Tityus obscurus novel putative na channel scorpion toxins
PLOS ONE, 2012Co-Authors: Jimmy Alexander Guerrerovargas, Lourival D. Possani, Caroline B. F. Mourão, Veronica Quinterohernandez, Elisabeth F SchwartzAbstract:Background: Colombia and Brazil are affected by severe cases of scorpionism. In Colombia the most dangerous accidents are caused by Tityus pachyurus that is widely distributed around this country. In the Brazilian Amazonian region scorpion stings are a common event caused by Tityus obscurus. The main objective of this work was to perform the molecular cloning of the putative Na+-channel scorpion toxins (NaScTxs) from T. pachyurus and T. obscurus venom glands and to analyze their phylogenetic relationship with other known NaScTxs from Tityus species. Methodology/Principal Findings: cDNA libraries from venom glands of these two species were constructed and five nucleotide sequences from T. pachyurus were identified as putative modulators of Na+-channels, and were named Tpa4, Tpa5, Tpa6, Tpa7 and Tpa8; the latter being the first anti-insect excitatory b-class NaScTx in Tityus scorpion venom to be described. Fifteen sequences from T. obscurus were identified as putative NaScTxs, among which three had been previously described, and the others were named To4 to To15. The peptides Tpa4, Tpa5, Tpa6, To6, To7, To9, To10 and To14 are closely related to the a-class NaScTxs, whereas Tpa7, Tpa8, To4, To8, To12 and To15 sequences are more related to the b-class NaScTxs. To5 is possibly an arthropod specific toxin. To11 and To13 share sequence similarities with both a and b NaScTxs. By means of phylogenetic analysis using the Maximum Parsimony method and the known NaScTxs from Tityus species, these toxins were clustered into 14 distinct groups. Conclusions/Significance: This communication describes new putative NaScTxs from T. pachyurus and T. obscurus and their phylogenetic analysis. The results indicate clear geographic separation between scorpions of Tityus genus inhabiting the Amazonian and Mountain Andes regions and those distributed over the Southern of the Amazonian rainforest. Based on the consensus sequences for the different clusters, a new nomenclature for the NaScTxs is proposed.
Adriano M.c. Pimenta - One of the best experts on this subject based on the ideXlab platform.
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Potassium channel blockers from the venom of the Brazilian scorpion Tityus serrulatus (Lutz and Mello, 1922)
Toxicon, 2016Co-Authors: Marie-france Martin-eauclaire, Maria Elena De Lima, Adriano Pimenta, Pierre Bougis, Adriano M.c. PimentaAbstract:Potassium (K(+)) channels are trans-membrane proteins, which play a key role in cellular excitability and signal transduction pathways. Scorpion toxins blocking the ion-conducting pore from the external side have been invaluable probes to elucidate the structural, functional, and physio-pathological characteristics of these ion channels. This review will focus on the interaction between K(+) channels and their peptide blockers isolated from the venom of the scorpion Tityus serrulatus, which is considered as the most dangerous scorpion in Brazil, in particular in Minas-Gerais State, where many casualties are described each year. The primary mechanisms of action of these K(+) blockers will be discussed in correlation with their structure, very often non-canonical compared to those of other well known K(+) channels blockers purified from other scorpion venoms. Also, special attention will be brought to the most recent data obtained by proteomic and transcriptomic analyses on Tityus serrulatus venoms and venom glands.
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Moving pieces in a taxonomic puzzle: venom 2D-LC/MS and data clustering analyses to infer phylogenetic relationships in some scorpions from the Buthidae family (Scorpiones).
Toxicon, 2006Co-Authors: Danielle G Nascimento, Maria Elena De Lima, Marie-france Martin-eauclaire, Breno Rates, Daniel M Santos, Thiago Verano-braga, Adriano Barbosa-silva, Alexandre A A Dutra, Ilka Biondi, Adriano M.c. PimentaAbstract:The Buthidae is the most clinically important scorpion family, with over 500 species distributed worldwide. Taxonomical positions and phylogenetic relationships concerning the representative genera and species of this family have been mostly inferred based upon comparisons between morphological characters. Yet, some authors have performed such inferences by comparing some structural properties of a few selected molecules found in the venoms from these scorpions. Here, we propose a novel methodology pipeline designed to address these issues. We have analyzed the whole venoms from some species that exemplify peculiar cases in the Buthidae family (Tityus stigmurus, Tityus serrulatus, Tityus bahiensis, Leiurus quinquestriatus quinquestriatus and Leiurus quinquestriatus hebraeus), by means of a proteomic approach using a 2D-LC/MS technique. The molecules found in these venoms were clustered according to their physicochemical properties (molecular mass and hydrophobicity), by using the machine learning-based Weka software. The clusters assessment, along with the number of molecules found in a given cluster for each scorpion, which assigns for the venom and structural family complexities, respectively, was used to generate a phenetic correlation tree for positioning these species. Our results were in accordance with the classical taxonomy viewpoint, which places T. serrulatus and T. stigmurus as very close species, T. bahiensis as a less related species in the Tityus genus and L. q. quinquestriatus and L. q. hebraeus with small differences within the same species (L. quinquestriatus). Therefore, we believe that this is a well-suited method to determine venom complexities that reflect the scorpions' evolutionary history, which can be crucial to reconstruct their phylogeny through the molecular evolution of their venoms.
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Purification, amino-acid sequence and partial characterization of two toxins with anti-insect activity from the venom of the South American scorpion Tityus bahiensis (Buthidae)
Toxicon, 2001Co-Authors: Adriano M.c. Pimenta, Luiz Carlos C. Afonso, Suely G. Figueiredo, Herve Rochat, Evanguedes Kalapothakis, Marie-france Martin-eauclaire, Maria Elena De LimaAbstract:We report here the isolation by a two-step chromatographic procedure of two new toxins from the South American scorpion Tityus bahiensis. Their amino-acid sequences and some of their biological features were established. The two toxins have different biological properties. Toxin TbIT-I had almost no activity or pharmacological effects in vertebrate tissues whereas it was lethal to house flies (LD50 80.0 ng/house fly). In contrast, Tb2-II was active against both mammals (intracerebroventricular injection of 100 ng/mouse was lethal) and insects (LD50 40.0 ng/house fly). The amino-acid sequences of these toxins were established and found to be similar (60-95%) to previously described β-toxins from the Tityus genus. Based on the available comparative information, this study attempts identify possible structure-function relationships that may be responsible for the differences in bioactivity displayed by these toxins. © 2001 Published by Elsevier Science Ltd.
Adolfo Borges - One of the best experts on this subject based on the ideXlab platform.
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molecular systematics of the neotropical scorpion genus Tityus buthidae the historical biogeography and venom antigenic diversity of toxic venezuelan species
Toxicon, 2010Co-Authors: Adolfo Borges, Eldredge Bermingham, Nimiadina Herrera, Marcelo J Alfonzo, Oris I SanjurAbstract:We provide a mitochondrial DNA-based phylogenetic hypothesis for 21 Tityus species collected in Venezuela, Trinidad, Brazil and Panama, including 12 taxa known to be toxic to humans. Our phylogenetic reconstruction is based on 850 nucleotides of the combined cytochrome oxidase subunit I and 16S rRNA genes for most species, and centered on Venezuelan scorpions owing to the detailed taxonomic and biogeographic information available for Tityus in this region. The principal phylogenetic result was the strong support for mtDNA clades representing geographical groupings associated with the Perija mountain range, the Merida Andes, or the central and eastern coastal ranges in Venezuela, suggesting that vicariance has been a potent force in the diversification of local scorpions. Venezuelan Tityus species have been organized by Gonzalez-Sponga into three artificial morphological groups, "androcottoides", "discrepans", and "nematochirus", based on the array of ventral carinae in metasomal segments II-IV. We also incorporated a fourth morphological group ("Tityus clathratus"), recently documented in Venezuela. Our results do not support the clustering of the species in the "androcottoides" and "discrepans" morphological groups, which include the majority of taxa of medical importance, but provided support for the "nematochirus" species group. T. clathratus was found to cluster with the Brazilian T. serrulatus and T. bahiensis. Divergence times of most clades are consistent with major events in the geological history of northern Venezuela and suggest that many Venezuelan Tityus species formed in the late Miocene and the Pliocene. In turn, we used the Tityus mtDNA phylogeny to determine the potential utility of phylogenetic systematics to predict Tityus venom antigenic reactivity by testing the recognition of T. nororientalis, T. discrepans, T. zulianus, T. perijanensis, and T. clathratus venoms by anti-T. discrepans horse antibodies. Cross-reactivity was significantly higher for the closely related eastern (T. nororientalis) and central coastal (T. discrepans) species in comparison to the distantly related Andean (T. zulianus) and Perija (T. perijanensis) species. Reactivity of T. clathratus low mol. mass toxic components towards anti-T. serrulatus and anti-T. discrepans antivenoms was low, suggesting that venom components produced by the subgenus ArchaeoTityus (which encompass "clathratus" species) diverge antigenically from other Tityus scorpions.
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discovery and description of the male of Tityus uquirensis scorpiones buthidae from the paria peninsula northeastern venezuela
Zootaxa, 2008Co-Authors: Leonardo De Sousa, Jesus Manzanilla, Adolfo Borges, Pablo Cornejoescobar, Tonio GregorianiAbstract:The male specimen of Tityus uquirensis Gonzalez-Sponga, 2001, a buthid scorpion species endemic to the Paria Peninsula, Sucre State, eastern Venezuela, is described for the first time. The male differs from the female in having elongated and slender pedipalps, a character also found in the males of T. nematochirus, T. meridanus, T. surmeridensis, and T. quirogae. Data are provided on T. uquirensis biology and morphological variations. Tityus uquirensis is the second northeastern Venezuelan scorpion (together with T. quirogae) exhibiting elongated pedipalps. Tityus uquirensis geographical distribution is hereby extended to the west, including the southern slope of the Paria Peninsula.
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second record of Tityus bahiensis scorpiones buthidae from venezuela epidemiological implications
Journal of Venomous Animals and Toxins Including Tropical Diseases, 2008Co-Authors: L. De Sousa, Jesus Manzanilla, Adolfo Borges, I Biondi, E AvellanedaAbstract:This work reports the second record of the scorpion Tityus bahiensis Perty from Venezuela. The specimen was found alive in a wardrobe at a hotel resort in Margarita Island, northeastern Venezuela. Morphological characterization allowed its assignment to the Tityus bahiensis population inhabiting the southernmost area of the species' geographic range, e.g. the state of Sao Paulo in Brazil, northern Argentina and Paraguay. The fact that the only available Venezuelan antiscorpion (anti-Tityus discrepans) serum does not neutralize the effects of alpha- and beta-toxin from Tityus serrulatus venom (which resembles in composition that of T. bahiensis) constitutes a warning to local clinicians confronted with envenomations by noxious species transported to Venezuela from Brazil by human agency.
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diversity of long chain toxins in Tityus zulianus and Tityus discrepans venoms scorpiones buthidae molecular immunological and mass spectral analyses
Comparative Biochemistry and Physiology C-toxicology & Pharmacology, 2006Co-Authors: Adolfo Borges, Marcelo J Alfonzo, Carmen C Garcia, Elizabeth Lugo, Michael J Jowers, Huub Op Den J M CampAbstract:In Venezuela, stings by Tityus zulianus scorpions produce cardiorespiratory arrest, whereas envenoming by Tityus discrepans involves gastrointestinal/pancreatic complications, suggesting structural and/or functional differences. We sought to compare their toxin repertoires through immunological, molecular, and mass spectral analyses. First, in vivo tests showed that neutralization of T. zulianus venom toxicity by the anti-T. discrepans antivenom was not complete. To compare T. discrepans and T. zulianus long-chain (sodium channel-active) toxins, their most toxic Sephadex® G-50 fractions, TdII and TzII, were subjected to acid–urea PAGE, which showed differences in composition. Amplification of toxin-encoding mRNAs using a leader peptide-based oligonucleotide rendered cDNAs representing twelve T. discrepans and two T. zulianus distinct toxin transcripts, including only one shared component, indicating divergence between T. zulianus and T. discrepans 5′ region-encoded, toxin signal peptides. A 3′-UTR polymorphism was also noticed among the transcripts encoding shared components Tz1 and Td4. MALDI–TOF MS profiling of TdII and TzII produced species-specific spectra, with seven of the individual masses matching those predicted by cDNA sequencing. Phylogenetic analysis showed that the unique T. zulianus transcript-encoded sequence, Tz2, is structurally related to Tityus serrulatus and Centruroides toxins. Together with previous reports, this work indicates that T. zulianus and T. discrepans toxin repertoires differ structurally and functionally.
