Toxins from Mamba Venoms that Facilitate Neuroiluscular Transmission

References

• Chapman D.S. The symptomatology, pathology, and treatment of the bites of venomous snakes of Central and South Africa, In Venomous Animals and Their Venoms, W. Bucherl, E. Buckley, V. Deulofeu. Academic Press, New York 1968; 463
   Google Scholar
• Irwin R. L., Oliver K. L., Mohamed A. H., Haast W. E. Toxicity of elapid venoms and an observation in relation to geographical location. Toxicon 1970; 8: 51
   Google Scholar
• Kabara J. J., Fischer G. Methodology for the isolation of low molecular weight toxins from snake venoms. Toxicon 1972; 10: 227
   Google Scholar
• Christensen P. A., Anderson C. G. Observations on Dendroaspis venoms. In Animal Toxins, F.E. Russell, P.R. Saunders. Pergamon Press, Oxford 1967; 223
   Google Scholar
• Excell B. J., Patel R. Characterization of toxic fractions from Dendroaspis. jamesoni venom. J. Physiol 1972; 225: 29
   Google Scholar
• Patel R., Excell B.J. The effects of lethal components of Dendroaspis jamesoni snake venom on neuromuscular transmission and on muscle membrane permeability. Toxicon 1975; 13: 295
   Google Scholar
• Shipolini R. A., Bailey G. S., Edwardson J. A., Banks B. E.C. Separation and characterization of polypeptides from the venom of Dendroaspis viridis Eur. J. Biochem. 1973; 40: 337
   Google Scholar
• Zaki O. A., Khogali A., Zak F. Black mamba venom and its fractions. The histopathological changes produced. Arch. Path. 1970; 89: 30
   Google Scholar
• Patel R., Excell B. J. The modes of action of whole Dendroaspis iamesoni venom on skeletal nerve-muscle preparations. Toxicon 1974; 12: 577
   Google Scholar
• Osman O. H., Ismail M., El-Asmar M. F. Pharmacological studies of snake (Dendroaspis anqusticeps) venom. Toxicon 1973; 11: 185
   Google Scholar
• Welsh J. H. Acetylcholine in snake venoms. Animal Toxins, F.E. Russell, P.R. Saunders. Pergamon Press, Oxford 1967; 363
   Google Scholar
• Barrett J. C., Harvey A. L. Effects of the venom of the green mamba, Dendroaspis anqusticeps. on skeletal muscle and neuromuscular transmission. Br. J. Pharmac. 1979; 67: 199
   PubMed Web of Science ®Google Scholar
• Strydom D. J., Botes D. P. Snake venom toxins-I. Preliminary studies on the separation of toxins of Elapidae snakes, Toxicon 1970; 8: 203
   Google Scholar
• Strydom D. J. Snake venom toxins. The amino acid sequences of two toxins from Dendroaspis polylepis polylepis (black mamba) venom. J. biol. Chem. 1972; 247: 4029
   Google Scholar
• Banks B. E.C., Miledi R., Shipolini R. A. The primary sequences and neuromuscular effects of three neurotoxic polypeptides from the venom of Dendroaspis viridis. Eur. J. Bipchem. 1974; 45: 457
   PubMedGoogle Scholar
• Bechis G., Granier C, Van Rietschoten J., Jover E., Rochat H., Miranda F. Purification of six neurotoxins from the venom of Dendroaspis viridis. Primary structure of two long toxins. Eur. J. Biochem. 1976; 68: 445
   Google Scholar
• Strydom A. J.C. Snake venom toxins. The amino acid sequences of two toxins from Dendroaspis jamesoni kaimosae (Jameson's mamba) venom. Biochim. Biophys. Acta 1973; 328: 491
   Google Scholar
• Harvey A. L., Karlsson E. Dendrotoxin from the venom of the green mamba, Dendroaspis anqusticeps. A neuretpxin that enhances acetylcholine release at neuromuscular junctions. Naunyn-Schmiedeberg's Arch. Pharmacol. 1980; 312: 1
   Google Scholar
• Dufton M. J., Hider R. C. Conformational properties of the neurotoxins and cytotoxins isolated from elapid snake venoms. Crit. Review Biochem. 1983; 14: 113
   PubMed Web of Science ®Google Scholar
• Joubert F. J., Taljaard N. Some properties and the complete primary structures of two reduced and S-carboxy-methylated polypeptides (S5C1. and S5C10) from Dendroaspis jamesoni kaimosae (Jamesons mamba) venom, Biochim. Biophys. Acta 1979; 579: 228
   PubMed Web of Science ®Google Scholar
• Kim H. S., Tamiya N. The amino acid sequence and position of the free thiol group of a short- chain neurotoxin from the common death-adder (Acanthophis antarcticus) venom. Biochem. J. 1981; 199: 211
   PubMedGoogle Scholar
• Harvey A. L., Hider R. C., Hodges S. J., Joubert F.J. Structure-activity studies of homologues of short chain neurotoxins from elapid snake venoms. Br. J. Pharmac. 1984, In press
   Google Scholar
• Rousselet A., Grazyna F., Boulain J.-C., Menez A. The interaction of neurotoxin derivatives with either acetylcholine receptor or a monoclonal antibody: an ESR study. Eur. J. Biochem. 1984, In press
   Google Scholar
• Tsetlin V. I., Karlsson E., Utkin Yu.N., Pluzhnikov K. A., Arseniev A. S., Surin A. M., Kondakov V. V., Bystrov V. F., Ivanov V. T., Ovchinnikov Yu. A. Interacting surfaces of neurotoxins and acetylcholine receptor. Toxicon 1981; 20: 83
   Google Scholar
• Karlsson E. Chemistry of protein toxins in snake venoms, In Handbook Exp. Pharmacol. Vol. 52, C.Y. Lee. Springer-Verlag, Berlin 1979; 159
   Google Scholar
• Chang C. C. The action of snake venoms on nerve and muscle. In Handbook Exp. Pharmacol. Vol. 52, C.Y. Lee. Springer-Verlag, Berlin 1979; 309
   Google Scholar
• Albuquerque E. X., Eldefrawi A. T., Eldefrawi M. E. The use of snake toxins for the study of the acetylcholine receptor and its ion-conductance modulator, In Handbook Exp. Pharmacol, vol. 52, C.Y. Lee. Springer-Verlag, Berlin 1979; 377
   Google Scholar
• Viljoen C. C., Botes D. P. Snake venom toxins. The purification and the amino acid sequence of toxin F.VII. from Dendroaspis anqusticeps venom. J. biol. Chem. 1973; 248: 4915
   PubMed Web of Science ®Google Scholar
• Viljoen C. C., Botes D.P. Snake venom toxins. The purification and amino acid sequence of toxin Ta2 from Dendroaspis anqusticeps venom. J. biol. Chem. 1974; 249: 366
   PubMed Web of Science ®Google Scholar
• Strydom D. J. Snake venom toxins. Purification and properties of low-molecular-weight polypeptides of Dendroaspis polylepis polylepis (black mamba) venom. Eur. J. Biochem. 1976; 69: 169
   PubMedGoogle Scholar
• Shipolini R. A., Banks B. E.C. The amino-acid sequence of a polypeptide from the venom of Dendroaspis viridis. Eur. J. Biochem. 1974; 49: 399
   Google Scholar
• Strydom D. J. Snake venom toxins. The amino-acid sequence of a short-neurotoxin homologue from Dendroaspis polylepis polylepis (black mamba) venom. Eur. J. Biochem. 1977; 76: 99
   Google Scholar
• Joubert F. J., Taljaard N. Snake venoms. The complete primary structures of two reduced and S-carboxymethylated angusticeps-type toxins from Dendroaspis angusticeps, Biochim. Biophys. Acta 1980; 623: 449
   Google Scholar
• Joubert F. J., Strydom A. J.C., Taljaard N. Snake venoms. The amino-acid sequence of protein S5C4. from Dendroaspis jamesoni kaimosae (Jameson's mamba; venom, Hoppe-Seyler's. Z. Physiol. Chem 1978; 359: 741
   Google Scholar
• Joubert F. J., Taljaard N. The primary structure of a short neurotoxin homologue (S4C8) from Dendroaspis jamesoni kaimosae (Jameson's mamba) venom, Int. J. Biochem 1980; 12: 567
   Google Scholar
• Joubert F. J., Taljaard N. The complete primary structure of toxin C from Dendroaspis polylepis polylepis (black mamba) venom. S. Afr. J. Chem. 1978; 31: 107
   Google Scholar
• Ryden L., Gabel D., Eaker D. A model of the three-dimensional structure of snake venom neurotoxins based on chemical evidence. Int. J. Pept. Prot. Res. 1973; 5: 261
   PubMedGoogle Scholar
• Szczepaniak A. C. Effect of a-bungarotoxin and Dendroaspis neurotoxins on acetylcholine responses of snail neurones. J. Physiol 1974; 241: 55P
   Google Scholar
• Lee C. Y., Tsaur M. L., Tsai M. C., Carlsson F. H.H., Joubert F. J. Facilitation of acetylcholine release by angusticeps-type toxins from mamba venom. Symposium Arcachon 1983; 25
   Google Scholar
• Karlsson E., Mbugua P. M., Rodriquez-Ithurralde D. Fasciculins, anti-cholinesterase toxins from the venom of the green mamba Dendroaspis anqusticeps. J. Physiol., Paris 1984, In press
   Google Scholar
• Joubert F. J., Taljaard N. Snake venoms. The amino-acid sequence of protein S2C4 from Dendroaspis jamesoni kaimosae (Jameson's mamba) venom. Hoppe-Seyler's Z. Physiol. Chem. 1979; 360: 571
   PubMedGoogle Scholar
• Joubert F. J., Viljoen C. C. Snake venoms. The amino-acid sequence of two reduced and S-carboxymethylated proteins (C8S2 and C9S3) from Dendroaspis anqusticeps venom, Hoppe-Seyler's Z. Physiol. Chem 1979; 360: 1075
   PubMedGoogle Scholar
• Joubert F. J., Taljaard N. Snake venoms. The amino acid sequences of two proteinase inhibitor homologues from Dendroaspis anqusticeps venom. Hoppe-Seyler's Z. Physiol. Chem. 1980; 361: 661
   PubMedGoogle Scholar
• Harvey A. L., Anderson A. J., Karlsson E. Facilitation of transmitter release by neurotoxins from snake venoms. J. Physiol., Paris. 1984, In press
   Google Scholar
• Harvey A. L., Gage P. W. Increase of evoked release of acetylcholine at the neuromuscular junction by a fraction from the venom of the Eastern green mamba snake (Dendroaspis anqusticeps). Toxicon 1981; 19: 373
   Google Scholar
• Rodriquez-Ithurralde D., Silveira R., Barbeito L., Dajas F. Fasciculin, a powerful anticholinesterase polypeptide from Dendroaspis angusticeps venom. Neurochem. Internat. 1983; 5: 267
   Google Scholar
• Harvey A. L., Karlsson E. Protease inhibitor homologues from mamba venoms: facilitation of acetylcholine release and interaction with prejunctional blocking toxins. Br. J. Pharmac. 1982; 77: 153
   PubMed Web of Science ®Google Scholar
• Othman I. B., Spokes J. W., Dolly J. O. Preparation of neurotoxic 3H-B-bungarotoxin. Demonstration of saturable binding to brain synapses and its inhibition by toxin. I. Eur. J. Biochem. 1982; 128: 267
   PubMedGoogle Scholar
• Strydom D. J. Protease inhibitors as snake venom toxins. Nature New Biol. 1972; 243: 88
   Google Scholar
• Black J. D., Othman I. B., Dolly J. O. Botulinum neurotoxin and dendrotoxin as probes for studies on transmitter release. J. Physiol., Paris 1984, In press
   Google Scholar
• Docherty R. J., Dolly J. O., Halliwell J. V., Othman I. Excitatory effects of dendrotoxin on the hippocampus in vitro. J. Physiol 1983; 336: 58P
   Google Scholar
• Harvey A. L., Karlsson E. Polypeptide neurotoxins from mamba venoms that facilitate transmitter release. Trends Pharmacol. Sci. 1984; 5: 71
   Web of Science ®Google Scholar
• Joubert F. J., Strydom D. J. Snake venoms. The amino-acid sequence of trypsin inhibitor E of Dendroaspis polylepis polylepis (black mamba) venom. Eur. J. Biochem. 1978; 87: 191
   Google Scholar
• Strydom D. J., Joubert F. J. The amino acid sequence of a weak trypsin inhibitor B from Dendroaspis polylepis polylepis (black mamba) venom. Hoppe-Seyler's Z. Physiol. Chem. 1981; 362: 1377
   Google Scholar
• Kassell B., Radicevic M., Ansfield M. J., Laskowski M. The basic trypsin inhibitor of bovine pancreas. IV. The linear sequence of the 58 amino acids. Biochem. Biophys. Res. Comm 1965; 18: 255
   PubMed Web of Science ®Google Scholar
• Huber R., Kukla D., Ruhlmann A., Steigemann W. Pancreatic trypsin inhibitor (Kunitz) Part I: structure and function. Cold Spring Harbor Symp. Quant. Biol. 1971; 36: 141
   Google Scholar
• Deisenhofer J., Steigemann W. Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at 1.5 8 resolution. Acta Cryst. B 1975; 31: 238
   Web of Science ®Google Scholar
• Wagner G., Wuthrich I. K. Sequential resonance assignments in protein H nuclear magnetic resonance spectra. Basic pancreatic trypsin inhibitor. J. Mol. Biol. 1982; 155: 347
   PubMed Web of Science ®Google Scholar
• Areniev A. S., Wider G., Joubert F. J., Wuthrich K. Assignment of the 'H nuclear magnetic resonance spectrum of the trypsin inhibitor E from Dendroaspis polylepis polylepis. Two-dimensional nuclear magnetic resonance at 500MHz. J. Mol. Biol 1982; 159: 323
   Google Scholar
• Pardi A., Wagner G., Wuthrich K. Protein conformation and proton nuclear-magnetic-resonance chemical shifts. Eur. J. Biochem. 1983; 137: 445
   PubMedGoogle Scholar
• Hollecker M., Creighton T. E., Gabriel M. Preliminary circular dichroism study of the conformations of intermediates trapped during protein folding. Biochimie 1981; 63: 835
   Google Scholar
• Hollecker M., Creighton T. E. Evolutionary conservation and variation of protein folding pathways. Two protease inhibitor homologues from black mamba venom. J. Mol. Biol. 1983; 168: 409
   PubMedGoogle Scholar
• Kondo K., Narita K., Lee C. Y. Amino acid sequences of the two polypeptide chains in β1-bungarotoxin from the venom of Bungarus multicinctus. J. Biochem., Tokyo 1978; 83: 101
   PubMed Web of Science ®Google Scholar
• Kondo K., Toda H., Narita K., Lee C.-Y. Amino acid sequence of β2-bungarotoxin from Bungarus multicinctus venom. The amino acid substitutions in the B chains. J. Biochem., Tokyo 1982; 91: 1519
   PubMed Web of Science ®Google Scholar
• Hokama Y., Iwanaga S., Tatsuki T., Suzuki T. Snake venom proteinase inhibitors. III. Isolation of five polypeptide inhibitors from the venoms of Hemachatus haemachatus (Ringhals cobra) and Naja nivea (Cape cobra) and the complete amino acid sequences of two of them. J. Biochem. Tokyo 1976; 79: 559
   Google Scholar
• Liu C. S., Wu T. C., Lo T. B. Complete amino acid sequences of two protease inhibitors in the venom of Bungarus fasciatus. Int. J. Peptide Protein Res. 1983; 21: 209
   Google Scholar
• Laskowski M., Jr., Kato I. Protein inhibitors of proteinases. Ann. Rev. Biochem. 1980; 49: 593
   PubMed Web of Science ®Google Scholar
• Jering H., Tschesche H. Replacement of lysine by arginine, phenylalanine and tryptophan in the reactive site of the bovine trypsin-kallikrein inhibitor (Kunitz) and the change of inhibitory properties. Eur. J. Biochem. 1976; 61: 453
   Google Scholar
• Takahashi H., Iwanaga S., Hokama Y., Suzuki T., Kitagawa T. Primary structure of proteinase inhibitor II isolated from the venom of Russell's viper (Vipera russelli). FEBS Lett. 1974; 38: 217
   Google Scholar
• Liu C.-S., Ho C.-L., Lee M.-T., Wu T.-C., Lo T.-B. Isolation and characterization of neurotoxins and protease inhibitors in the venom of Bungarus fasciatus, Proc. Nat. Sci. Counc. B, ROC 1981; 5: 355
   Google Scholar
• Rodriquez-Ithurralde D., Silveira R., Barbeito L., Dajas F. Gel chromatography and anticholinesterase activity of Dendroaspis anqusticeps venom. Braz. J. Med. Biol. Sci. 1981; 14: 367
   Google Scholar
• Wangai J., Thairu K., Bharaj B. S., Telang B. V. Identification and isolation of three acetylcholinesterase inactivating fractions in the venom of Dendroaspis angusticeps. Acta Physiol. Acad. Scient- Hung. 1982; 60: 83
   Google Scholar
• Wangai J., Thairu K., Bharaj B. S., Telang B. V. Pharmacological evaluation and molecular weight determination of acetylcholinesterase inhibiting fractions in the venom of Dendroaspis angusticeps. Acta Physiol. Acad. Scient. Hung. 1982; 60: 75
   Google Scholar
• Krebs H. A., Henseleit K. Untersuchungen uber die Harnstoffbildung im Tierkorper. Hoppe-Seyler's Z. Physiol. Chem. 1932; 210: 33
   Google Scholar
• Augustinsson K. B., Eriksson H., Faijersson Y. A new approach to determining cholinesterase activities in samples of whole blood, Clin. Chim. Acta 1978; 89: 239
   Google Scholar
• Taylor P., Lwebuga-Mukusa J., Lappi S., Rademacher J. Propidium - a fluorescent probe for a peripheral anionic site on acetylcholinesterase. Mol. Pharmacol. 1974; 10: 703
   Web of Science ®Google Scholar
• Dixon M. The graphical determination of Km and Ki Biochem. J. 1972; 129: 197
   Google Scholar
• Bowman W. C. Anticholinesterase drugs in the fowl, In Physiology of the Domestic Fowl, C. Horton-Smith, E.C. Amroso. Oliver & Boyd, Edinburgh 1966; 249
   Google Scholar
• Agbaji A. A., Gerassimidis K., Hider R. C. A comparison of eel electroplax and snake acetylcholinesterases. J. Comp. Physiol. 1984, In press
   Google Scholar
• Lee C.-Y., Chen Y. M., Joubert F. J. Protection by atropine against lethal effects of the anqusticeps-type toxin Fy from Eastern green mamba venom and toxin I from black mamba venom. Toxicon 1982; 20: 665
   Google Scholar
• Lin Shiau S. Y., Liao C., Lee C.-Y. Mechanism of anti-cholinesterase activities of cardiotoxin. protamine and polylysine, Biochem. J. 1977; 161: 229
   Google Scholar