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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.
Marie-France Martin-Eauclaire; Sonia Adi-Bessalem; Djelila Hammoudi-Triki; Fatima Laraba-Djebari; Pierre E. Bougis. Serotherapy against Voltage-Gated Sodium Channel-Targeting α-Toxins from Androctonus Scorpion Venom. Toxins 2019, 11, 63 .
AMA StyleMarie-France Martin-Eauclaire, Sonia Adi-Bessalem, Djelila Hammoudi-Triki, Fatima Laraba-Djebari, Pierre E. Bougis. Serotherapy against Voltage-Gated Sodium Channel-Targeting α-Toxins from Androctonus Scorpion Venom. Toxins. 2019; 11 (2):63.
Chicago/Turabian StyleMarie-France Martin-Eauclaire; Sonia Adi-Bessalem; Djelila Hammoudi-Triki; Fatima Laraba-Djebari; Pierre E. Bougis. 2019. "Serotherapy against Voltage-Gated Sodium Channel-Targeting α-Toxins from Androctonus Scorpion Venom." Toxins 11, no. 2: 63.
The Tityus serrulatus scorpion species represents a serious human health threat to in Brazil because it is among the animals that produces the most dangerous venoms for mammals in South America. Its venom has provided several highly selective ligands that specifically interact with sodium and potassium channels. During the past decades, several international groups published an increasing amount of data on the isolation and the chemical, pharmacological and immunological characterisation of its main β-toxin, Ts1. In this review, we compiled the best available past and recent knowledge on Ts1. Aside from its intricate purification, the state-of-the-art understanding concerning its pharmacological activities is presented. Its solved three-dimensional structure is shown, as well as the possible surface areas of contact between Ts1 and its diverse voltage-gated Na+ channel targets. Organisations of the gene and the precursor encoding Ts1 are also tackled based on available cDNA clones or on information obtained from polymerase chain reactions of stretches of scorpion DNA. At last, the immunological studies complete with Ts1 to set up an efficient immunotherapy against the Tityus serrulatus venom are summarised.
Marie-France Martin-Eauclaire; Pierre E. Bougis; Maria Elena De Lima. Ts1 from the Brazilian scorpion Tityus serrulatus: A half-century of studies on a multifunctional beta like-toxin. Toxicon 2018, 152, 106 -120.
AMA StyleMarie-France Martin-Eauclaire, Pierre E. Bougis, Maria Elena De Lima. Ts1 from the Brazilian scorpion Tityus serrulatus: A half-century of studies on a multifunctional beta like-toxin. Toxicon. 2018; 152 ():106-120.
Chicago/Turabian StyleMarie-France Martin-Eauclaire; Pierre E. Bougis; Maria Elena De Lima. 2018. "Ts1 from the Brazilian scorpion Tityus serrulatus: A half-century of studies on a multifunctional beta like-toxin." Toxicon 152, no. : 106-120.
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.
Marie-France Martin-Eauclaire; Juan Salvatierra; Frank Bosmans; Pierre E. Bougis. The scorpion toxin Bot IX is a potent member of the α-like family and has a unique N-terminal sequence extension. FEBS Letters 2016, 590, 3221 -3232.
AMA StyleMarie-France Martin-Eauclaire, Juan Salvatierra, Frank Bosmans, Pierre E. Bougis. The scorpion toxin Bot IX is a potent member of the α-like family and has a unique N-terminal sequence extension. FEBS Letters. 2016; 590 (18):3221-3232.
Chicago/Turabian StyleMarie-France Martin-Eauclaire; Juan Salvatierra; Frank Bosmans; Pierre E. Bougis. 2016. "The scorpion toxin Bot IX is a potent member of the α-like family and has a unique N-terminal sequence extension." FEBS Letters 590, no. 18: 3221-3232.
Mass spectrometry (MS) is at present well recognized as a method of choice for the study of any venoms. As a most basic venomic analysis, venom mass fingerprinting (VMF) which depicts the venom’s all-inclusive masses may be very informative when comparisons among close or distant venomous species have to be pictured, as well as intraspecific venom variations. This chapter reports, as an example, the technological requirements and pitfalls using the state-of-the-art nano-ultrahigh-performance liquid chromatography (UHPLC) and matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) MS in order to achieve in 2-h at the best and from tens of venom nanograms only a full-automated workflow. Lastly, having the opportunity of acquiring VMF in such a fast and easy way could be extremely valuable for carrying out phylogenetic studies based on mass clades.
Pierre E. Bougis. Automated Mass Fingerprinting of Venoms in Nanogram Range: Review of Technology. Venom Genomics and Proteomics 2016, 307 -316.
AMA StylePierre E. Bougis. Automated Mass Fingerprinting of Venoms in Nanogram Range: Review of Technology. Venom Genomics and Proteomics. 2016; ():307-316.
Chicago/Turabian StylePierre E. Bougis. 2016. "Automated Mass Fingerprinting of Venoms in Nanogram Range: Review of Technology." Venom Genomics and Proteomics , no. : 307-316.
Pierre Edouard Bougis; Marie-France Martin-Eauclaire. Shal-type (Kv4.x) potassium channel pore blockers from scorpion venoms. Sheng li xue bao : [Acta physiologica Sinica] 2015, 67, 1 .
AMA StylePierre Edouard Bougis, Marie-France Martin-Eauclaire. Shal-type (Kv4.x) potassium channel pore blockers from scorpion venoms. Sheng li xue bao : [Acta physiologica Sinica]. 2015; 67 (3):1.
Chicago/Turabian StylePierre Edouard Bougis; Marie-France Martin-Eauclaire. 2015. "Shal-type (Kv4.x) potassium channel pore blockers from scorpion venoms." Sheng li xue bao : [Acta physiologica Sinica] 67, no. 3: 1.
Animal toxins that inhibit voltage-gated sodium (Nav) channel fast inactivation can do so through an interaction with the S3b–S4 helix-turn-helix region, or paddle motif, located in the domain IV voltage sensor. Here, we used surface plasmon resonance (SPR), an optical approach that uses polarized light to measure the refractive index near a sensor surface to which a molecule of interest is attached, to analyze interactions between the isolated domain IV paddle and Nav channel–selective α-scorpion toxins. Our SPR analyses showed that the domain IV paddle can be removed from the Nav channel and immobilized on sensor chips, and suggest that the isolated motif remains susceptible to animal toxins that target the domain IV voltage sensor. As such, our results uncover the inherent pharmacological sensitivities of the isolated domain IV paddle motif, which may be exploited to develop a label-free SPR approach for discovering ligands that target this region.
Marie-France Martin-Eauclaire; Géraldine Ferracci; Frank Bosmans; Pierre E. Bougis. A surface plasmon resonance approach to monitor toxin interactions with an isolated voltage-gated sodium channel paddle motif. Journal of General Physiology 2015, 145, 155 -162.
AMA StyleMarie-France Martin-Eauclaire, Géraldine Ferracci, Frank Bosmans, Pierre E. Bougis. A surface plasmon resonance approach to monitor toxin interactions with an isolated voltage-gated sodium channel paddle motif. Journal of General Physiology. 2015; 145 (2):155-162.
Chicago/Turabian StyleMarie-France Martin-Eauclaire; Géraldine Ferracci; Frank Bosmans; Pierre E. Bougis. 2015. "A surface plasmon resonance approach to monitor toxin interactions with an isolated voltage-gated sodium channel paddle motif." Journal of General Physiology 145, no. 2: 155-162.
Jean-Pierre Rosso; Jürgen R. Schwarz; Marcelo Diaz-Bustamante; Brigitte Céard; José María Gutiérrez; Matthias Kneussel; Olaf Pongs; Frank Bosmans; Pierre E. Bougis. MmTX1 and MmTX2 from Coral Snake Venom Potently Modulate GABA(A) Receptor Activity. Biophysical Journal 2015, 108, 434a .
AMA StyleJean-Pierre Rosso, Jürgen R. Schwarz, Marcelo Diaz-Bustamante, Brigitte Céard, José María Gutiérrez, Matthias Kneussel, Olaf Pongs, Frank Bosmans, Pierre E. Bougis. MmTX1 and MmTX2 from Coral Snake Venom Potently Modulate GABA(A) Receptor Activity. Biophysical Journal. 2015; 108 (2):434a.
Chicago/Turabian StyleJean-Pierre Rosso; Jürgen R. Schwarz; Marcelo Diaz-Bustamante; Brigitte Céard; José María Gutiérrez; Matthias Kneussel; Olaf Pongs; Frank Bosmans; Pierre E. Bougis. 2015. "MmTX1 and MmTX2 from Coral Snake Venom Potently Modulate GABA(A) Receptor Activity." Biophysical Journal 108, no. 2: 434a.
Even though Buthus occitanus scorpions are found throughout the Mediterranean region, a lack of distinctive characteristics has hampered their classification into different subspecies. Yet, stings from this particular scorpion family are reported each year to result in pain followed by various toxic symptoms. In order to determine the toxicity origin of the rare French B. occitanus Amoreux scorpion, we collected several specimens and studied their venom composition using a nano ultra high performance liquid chromatography and matrix assisted laser desorption/ionisation time-of-flight mass spectrometry (nano UHPLC/MALDI-TOF-MS) automated workflow combined with an enzyme-linked immunosorbent assay (ELISA) approach. Moreover, we compared this dataset to that obtained from highly lethal Androctonus australis and Androctonus mauretanicus scorpions collected in North Africa. As a result, we found that the B. occitanus Amoreux venom is toxic to mice, an observation that is most likely caused by venom components that inhibit voltage-gated sodium channel inactivation. Moreover, we identified similarities in venom composition between B. occitanus scorpions living in the South of France and other Buthidae collected in Morocco and Algeria. As such, the results of this study should be taken into consideration when treating stings from the B. occitanus species living in the South of France.
Marie-France Martin-Eauclaire; Frank Bosmans; Brigitte Céard; Sylvie Diochot; Pierre E. Bougis. A first exploration of the venom of the Buthus occitanus scorpion found in southern France. Toxicon 2014, 79, 55 -63.
AMA StyleMarie-France Martin-Eauclaire, Frank Bosmans, Brigitte Céard, Sylvie Diochot, Pierre E. Bougis. A first exploration of the venom of the Buthus occitanus scorpion found in southern France. Toxicon. 2014; 79 ():55-63.
Chicago/Turabian StyleMarie-France Martin-Eauclaire; Frank Bosmans; Brigitte Céard; Sylvie Diochot; Pierre E. Bougis. 2014. "A first exploration of the venom of the Buthus occitanus scorpion found in southern France." Toxicon 79, no. : 55-63.
The availability of a large variety of specific blockers, which inhibit different K(+) currents, would help to elucidate their differences in physiological function. Short peptide toxins isolated from scorpion venoms are able to block voltage-dependent or Ca(2+)-activated K(+) channels. Here, we have studied the venom of the Moroccan scorpion Buthus occitanus Paris (BoP) in order to find new peptides, which could enlarge our structure-function relationship knowledge on the Kv1.3 blocker Kaliotoxin (KTX) that belongs to the α-KTx3.1 family. Indeed and since more a decade, KTX is widely used by international investigators because it exhibits a quite sharp specificity and a high-affinity for the Kv1.3 channel, which is not only a neuronal channel but also a therapeutic target for diverse autoimmune diseases such as multiple sclerosis, type 1 diabetes, and rheumatoid arthritis. The BoP venom was first investigated using HPLC and MALDI-TOF/MS. Further, the HPLC fractions were screened by ELISA with antibodies raised against KTX. These antibodies recognized at least three components toxic in mice by intracerebroventricular injection. They were further pharmacologically characterized by competition using (125)I-KTX bound to its specific binding sites on rat brain synaptosomes. A single component (4161 Da) inhibited totally the (125)I-KTX binding and with high-affinity (IC50 = 0.1 nM), while the two other components poorly competed with (IC50 > 100 nM). These toxins were sequenced in full by Edman's degradation. The high-affinity ligand (BoPKTX) shares 86% sequence identity with KTX and was classified as toxin α-KTx3.17. The two others peptides (BoP1 and BoP2, 4093 Da and 4121 Da, respectively) only differ by a Lys/Arg mutation. Their amino acid sequences were related to Martentoxin, which has been characterized from the Chinese scorpion Buthus martenzi Karch and described as both a BKCa and Kv1.3 blocker. Accordingly, they belong to the α-KTx16 family.
Marie-France Martin-Eauclaire; Brigitte Céard; Maya Belghazi; Régine Lebrun; Pierre E. Bougis. Characterization of the first K+ channel blockers from the venom of the Moroccan scorpion Buthus occitanus Paris. Toxicon 2013, 75, 168 -176.
AMA StyleMarie-France Martin-Eauclaire, Brigitte Céard, Maya Belghazi, Régine Lebrun, Pierre E. Bougis. Characterization of the first K+ channel blockers from the venom of the Moroccan scorpion Buthus occitanus Paris. Toxicon. 2013; 75 ():168-176.
Chicago/Turabian StyleMarie-France Martin-Eauclaire; Brigitte Céard; Maya Belghazi; Régine Lebrun; Pierre E. Bougis. 2013. "Characterization of the first K+ channel blockers from the venom of the Moroccan scorpion Buthus occitanus Paris." Toxicon 75, no. : 168-176.
During the past decade mass spectrometry (MS) has become one of the major suitable techniques for peptide and protein analysis from animal venoms, not only to identify new toxins within these complex mixtures, but also for toxin structural studies. The goal of the experiments presented here was to test the ultimate limit for producing scorpion venom mass fingerprinting (VMF; i.e. a comprehensive list of all masses in presence). Thanks to recent developments in nano ultra high performance liquid chromatography (UHPLC) and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF/MS), we sought the experimental conditions for setting up an automated data acquisition workflow. As the main result, we demonstrate the possibility to easily achieve VMF having in hand only tens of nanogram of venom. ELISA on-line was also beneficial to monitor in the picogram range for toxin families using specific antisera raised against major toxins.
Marie-France Martin-Eauclaire; Samuel Granjeaud; Maya Belghazi; Pierre E. Bougis. Achieving automated scorpion venom mass fingerprinting (VMF) in the nanogram range. Toxicon 2013, 69, 211 -218.
AMA StyleMarie-France Martin-Eauclaire, Samuel Granjeaud, Maya Belghazi, Pierre E. Bougis. Achieving automated scorpion venom mass fingerprinting (VMF) in the nanogram range. Toxicon. 2013; 69 ():211-218.
Chicago/Turabian StyleMarie-France Martin-Eauclaire; Samuel Granjeaud; Maya Belghazi; Pierre E. Bougis. 2013. "Achieving automated scorpion venom mass fingerprinting (VMF) in the nanogram range." Toxicon 69, no. : 211-218.
K+ channels containing Kv4.2 and Kv4.3 pore-forming subunits mediate most of the subthreshold-operating somatodendritic A-type K+ current in CNS neurons. These channels are believed to be important in regulating the frequency of repetitive firing, the backpropagation of action potential into dendrites, and dendritic integration and plasticity. Moreover, they have been implicated in several diseases from pain to epilepsy and autism spectrum disorders. The lack of toxins that specifically and efficiently block these channels has hampered studies aimed at confirming their functional role and their involvement in disease. AmmTX3 and other related members of the α-KTX15 family of scorpion toxins have been shown to block the A-type K+ current in cultured neurons, but their specificity has been questioned because the toxins do not efficiently block the currents mediated by Kv4.2 or Kv4.3 subunits expressed in heterologous cells. Here we show that the high-affinity blockade of Kv4.2 and Kv4.3 channels by AmmTX3 depends on the presence of the auxiliary subunits DPP6 and DPP10. These proteins are thought to be components of the Kv4 channel complex in neurons and to be important for channel expression in dendrites. These studies validate the use of AmmTX3 as a blocker of the Kv4-mediated A-type K+ current in neurons.
Jon K. Maffie; Elena Dvoretskova; Pierre Edouard Bougis; Marie-France Martin-Eauclaire; Bernardo Rudy. Dipeptidyl-peptidase-like-proteins confer high sensitivity to the scorpion toxin AmmTX3 to Kv4-mediated A-type K+channels. The Journal of Physiology 2013, 591, 2419 -2427.
AMA StyleJon K. Maffie, Elena Dvoretskova, Pierre Edouard Bougis, Marie-France Martin-Eauclaire, Bernardo Rudy. Dipeptidyl-peptidase-like-proteins confer high sensitivity to the scorpion toxin AmmTX3 to Kv4-mediated A-type K+channels. The Journal of Physiology. 2013; 591 (10):2419-2427.
Chicago/Turabian StyleJon K. Maffie; Elena Dvoretskova; Pierre Edouard Bougis; Marie-France Martin-Eauclaire; Bernardo Rudy. 2013. "Dipeptidyl-peptidase-like-proteins confer high sensitivity to the scorpion toxin AmmTX3 to Kv4-mediated A-type K+channels." The Journal of Physiology 591, no. 10: 2419-2427.
Marie-France Martin-Eauclaire; Najwa Abbas; Pierre E. Bougis; Régis Guieu. 176. Is the Endogenous Opioid System Involved in the Antalgic Effect of Scorpion Toxins in Mice? Toxicon 2012, 60, 186 .
AMA StyleMarie-France Martin-Eauclaire, Najwa Abbas, Pierre E. Bougis, Régis Guieu. 176. Is the Endogenous Opioid System Involved in the Antalgic Effect of Scorpion Toxins in Mice? Toxicon. 2012; 60 (2):186.
Chicago/Turabian StyleMarie-France Martin-Eauclaire; Najwa Abbas; Pierre E. Bougis; Régis Guieu. 2012. "176. Is the Endogenous Opioid System Involved in the Antalgic Effect of Scorpion Toxins in Mice?" Toxicon 60, no. 2: 186.
Marie-France Martin-Eauclaire; Pierre E. Bougis. 179. Automated Mass Fingerprinting of Scorpion Venoms in the Nanogram Range. Toxicon 2012, 60, 187 .
AMA StyleMarie-France Martin-Eauclaire, Pierre E. Bougis. 179. Automated Mass Fingerprinting of Scorpion Venoms in the Nanogram Range. Toxicon. 2012; 60 (2):187.
Chicago/Turabian StyleMarie-France Martin-Eauclaire; Pierre E. Bougis. 2012. "179. Automated Mass Fingerprinting of Scorpion Venoms in the Nanogram Range." Toxicon 60, no. 2: 187.
In this paper were described the purification, the sequencing, and the immunological and biological characterization of a new Kaliotoxin analog, Aam-KTX, from the venom of the scorpion Androctonus amoreuxi. The toxin effects on three cloned Kv channels (Kv1.1, Kv1.2, and Kv1.3) were investigated in Xenopus oocytes using electrophysiology experiments. The Aam-KTX preference for Kv1.3 channel versus Kv1.2 was expected (EC50 values, 1.1 ± 0.02 and 10.4 ± 1.5 nM, respectively) but its total inefficacity on Kv1.1 was very surprising. 3D molecular modeling of Aam-KTX brought putative answers to this difference in selectivity.
Najwa Abbas; Maya Belghazi; Yousra Abdel-Mottaleb; Jan Tytgat; Pierre E. Bougis; Marie-France Martin-Eauclaire. A new Kaliotoxin selective towards Kv1.3 and Kv1.2 but not Kv1.1 channels expressed in oocytes. Biochemical and Biophysical Research Communications 2008, 376, 525 -530.
AMA StyleNajwa Abbas, Maya Belghazi, Yousra Abdel-Mottaleb, Jan Tytgat, Pierre E. Bougis, Marie-France Martin-Eauclaire. A new Kaliotoxin selective towards Kv1.3 and Kv1.2 but not Kv1.1 channels expressed in oocytes. Biochemical and Biophysical Research Communications. 2008; 376 (3):525-530.
Chicago/Turabian StyleNajwa Abbas; Maya Belghazi; Yousra Abdel-Mottaleb; Jan Tytgat; Pierre E. Bougis; Marie-France Martin-Eauclaire. 2008. "A new Kaliotoxin selective towards Kv1.3 and Kv1.2 but not Kv1.1 channels expressed in oocytes." Biochemical and Biophysical Research Communications 376, no. 3: 525-530.
From the venom of the scorpion Androctonus australis, we have isolated a new bioactive polypeptide termed AaBTX-L1. When tested on the insect voltage-gated Na+ channel (para) of the fruit fly, this toxin was able to induce a clear shift in activation (V1/2), resulting in the opening of the channel at more negative membrane potentials. Furthermore, AaBTX-L1 was totally devoid of toxicity when injected into mice intracerebroventricularly and did not compete with radiolabeled voltage-gated K+ and Na+ channel toxins in binding experiments on rat brain synaptosomes. Using its N-terminal amino acid sequence to design degenerate primers, several clones were amplified by PCR from the A. australis venom gland cDNA library. As a consequence, seven full oligonucleotide sequences encoding “long-chain” polypeptides with only three disulfide bridges have been cloned for the first time and are described here. Remarkably, they share high similarity with the anti-insect toxin Birtoxin from Parabuthus transvaalicus.
Marie-France Martin-Eauclaire; Brigitte Céard; Frank Bosmans; Jean-Pierre Rosso; Jan Tytgat; Pierre E. Bougis. New “Birtoxin analogs” from Androctonus australis venom. Biochemical and Biophysical Research Communications 2005, 333, 524 -530.
AMA StyleMarie-France Martin-Eauclaire, Brigitte Céard, Frank Bosmans, Jean-Pierre Rosso, Jan Tytgat, Pierre E. Bougis. New “Birtoxin analogs” from Androctonus australis venom. Biochemical and Biophysical Research Communications. 2005; 333 (2):524-530.
Chicago/Turabian StyleMarie-France Martin-Eauclaire; Brigitte Céard; Frank Bosmans; Jean-Pierre Rosso; Jan Tytgat; Pierre E. Bougis. 2005. "New “Birtoxin analogs” from Androctonus australis venom." Biochemical and Biophysical Research Communications 333, no. 2: 524-530.
Brigitte Céard; Marie-France Martin-Eauclaire; Pierre E. Bougis. Evidence for a position-specific deletion as an evolutionary link between long- and short-chain scorpion toxins. FEBS Letters 2001, 494, 246 -248.
AMA StyleBrigitte Céard, Marie-France Martin-Eauclaire, Pierre E. Bougis. Evidence for a position-specific deletion as an evolutionary link between long- and short-chain scorpion toxins. FEBS Letters. 2001; 494 (3):246-248.
Chicago/Turabian StyleBrigitte Céard; Marie-France Martin-Eauclaire; Pierre E. Bougis. 2001. "Evidence for a position-specific deletion as an evolutionary link between long- and short-chain scorpion toxins." FEBS Letters 494, no. 3: 246-248.
New World elapids are coral snakes that belong to the genus Micrurus, and for which the venom biochemistry is mostly unknown. Analysis has been difficult because the coral snakes produce small quantities of venom. Clinical observations following bites show mainly neurotoxic effects. Experimentally, cardiotoxic, haemolytic and myotoxic activities are also reported. An experimental approach, using reverse-phase high-performance liquid chromatography and specific assays for alpha-neurotoxin and phospholipase A2 activities, was conducted on milligram quantities of venoms from three Micrurus species from Costa Rica; M. nigrocinctus nigrocinctus, M. alleni yatesi and M. multifasciatus. Neurotoxicity was determined by competition binding experiments with the Torpedo marmorata acetylcholine receptor. Phospholipase A2 activity was measured by fluorimetry using a pyrene lipid substrate. In this way, we purified and characterized seven alpha-neurotoxins, five phospholipases A2 and four toxin homologs. The amino acid sequence of the major alpha-neurotoxin from M. nigrocinctus nigrocinctus venom was fully determined and compared to Old Word representatives. Distance matrix data were generated to set up phylogeny relationships among elapid short-chain alpha-neurotoxins, which proved to be in accordance with the taxonomic classification and geographical distribution of snake species.UCR::Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP
Jean-Pierre Rosso; Orietta Vargas-Rosso; José María Gutiérrez; Hervé Rochat; Pierre E. Bougis. Characterization of alpha-Neurotoxin and Phospholipase A2 Activities from Micrurus Venoms. Determination of the Amino Acid Sequence and Receptor-Binding Ability of the Major alpha-Neurotoxin from Micrurus Nigrocinctus Nigrocinctus. JBIC Journal of Biological Inorganic Chemistry 1996, 238, 231 -239.
AMA StyleJean-Pierre Rosso, Orietta Vargas-Rosso, José María Gutiérrez, Hervé Rochat, Pierre E. Bougis. Characterization of alpha-Neurotoxin and Phospholipase A2 Activities from Micrurus Venoms. Determination of the Amino Acid Sequence and Receptor-Binding Ability of the Major alpha-Neurotoxin from Micrurus Nigrocinctus Nigrocinctus. JBIC Journal of Biological Inorganic Chemistry. 1996; 238 (1):231-239.
Chicago/Turabian StyleJean-Pierre Rosso; Orietta Vargas-Rosso; José María Gutiérrez; Hervé Rochat; Pierre E. Bougis. 1996. "Characterization of alpha-Neurotoxin and Phospholipase A2 Activities from Micrurus Venoms. Determination of the Amino Acid Sequence and Receptor-Binding Ability of the Major alpha-Neurotoxin from Micrurus Nigrocinctus Nigrocinctus." JBIC Journal of Biological Inorganic Chemistry 238, no. 1: 231-239.