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Structure and Function of Cobra Neurotoxin

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Natural Toxins 2

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 391))

Abstract

Snake neurotoxins are the main toxic proteins of cobra, krait, tiger snake and sea snake venoms which block neuromuscular transmission and cause animals death of respiratory paralysis. Snake neurotoxins are classified into two distinct types, postsynaptic and presynaptic neurotoxins, in relation to the neuromuscular junction. Postsynaptic neurotoxins bind specifically to nicotinic acetylcholine receptor (AChR) at the motor endplate and produce a nondepolarizing block of neuromuscular transmission. Presynaptic neurotoxins block the release of acetylcholine from the presynaptic motor nerve terminals.

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Reference

  • Basus, V.J., Song, G. and Hawrot, E. (1993) NMR solution structure of an a bungarotoxin/nicotinic receptor peptide complex. Biochemistry 32: 12290–12298.

    Article  PubMed  CAS  Google Scholar 

  • Blobel, G. and Dobberstein, B. (1975) Transfer of proteins across membrans. J. Cell Biol. 67: 835–851.

    Article  PubMed  CAS  Google Scholar 

  • Chang, C. C. and Yang, C. C. (1969) Immunochemical studies on cobrotoxin. J. Immunol. 102: 1437–1444.

    PubMed  CAS  Google Scholar 

  • Chang, C. C, Yang, C. C, Hamaguchi, K., Nakai, K. and Hayashi, K. (1971a) Studies on the status of tyrosyl residues in cobrotoxin. Biochim. Biophys. Acta 236: 164–173.

    CAS  Google Scholar 

  • Chang, C. C, Yang, C. C, Nakai, K. and Hayashi, K. (1971b) Studies on the status of free amino and carboxyl groups in cobrotoxin. Biochim. Biophys. Acta 251: 334–344.

    CAS  Google Scholar 

  • Chomczynski, R and Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162: 156–159.

    CAS  Google Scholar 

  • Dennis, M., Giraudat, J., Kotzyba-Hibert, F., Goeldner, M., Hirth, C, Chang, J.Y, Lazure, C, Chretien, M. and Changeux, J.R (1988) Amino acids of the Torpedo marmorata acetylcholine receptor a subunit labeled by a photoaffinity ligand for the acetylcholine binding site. Biochemistry 27: 2346–2357.

    CAS  Google Scholar 

  • Ducancel, R, Guignery-Frelat, G., Boulain, J.C. and Menez, A. (1990) Nucleotide sequence and structure analysis of cDNA encoding short-chain neurotoxins from venom glands of sea snake (Aipysurus laevis). Toxicon 28: 119–123.

    PubMed  CAS  Google Scholar 

  • Endo, T. and Tamiya, N. (1991) Structure-function relationships of postsynaptic neurotoxins from snake venoms, in “Snake Toxins” (Harvey, A.L., ed.) Pergamon Press, New York, pp. 165–222.

    Google Scholar 

  • Endo T., Oya, M., Tamiya, N. and Hayashi, K. (1987) Role of C-terminal tail of long neurotoxins from snake venoms in molecular conformation and acetylcholine receptor binding: Protein nuclear magnetic resonance and competition binding studies. Biochemistry 26: 4592–4598.

    Article  PubMed  CAS  Google Scholar 

  • Love, R. A. and Stroud, R. M. (1986) The crystal structure of a-bungarotoxin at 2.5 Ä resolution: Relation to solution structure and binding to acetylcholine receptor. Protein Eng. 1: 37–46.

    Article  PubMed  CAS  Google Scholar 

  • Low, B. W. and Corfield, P. W. R. (1986) Erabutoxin b: Structure–function relationships following initial protein refinement at 0.140-nm resolution. Eur. J. Biochem. 161: 579 –587.

    Article  PubMed  CAS  Google Scholar 

  • Low, B. W., Preston, H. S., Sato, A., Rosen, L. S., Searle, F. E., Rudko, A. D. and Richardson, J. S. (1976) Three dimensional structure of erabutoxin b neurotoxic protein: Inhibitor of acetylcholine receptor. Proc. Natl. Acad. Sci. USA 73: 2991–2994.

    Article  PubMed  CAS  Google Scholar 

  • Maniatis, T., Fritsch, E.F. and Sambrook, J. (1989) Molecular Cloning, A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y

    Google Scholar 

  • Martin, B. M., Chibber, B. A. and Maelicke, A. (1983) The sites of neurotoxicity in a-cobratoxin. J. Biol. Chem. 258: 8714–8722.

    Google Scholar 

  • Mebs, D. (1988) Snake venom toxins: Structural aspects, in “Neurotoxins in Neurochemistry” (Dolly, J. O., ed.) Ellis Horwood, Chichester, England, pp. 3–12.

    Google Scholar 

  • Mulac-Jericevic, B. and Atassi, M.Z. (1987) Profile of the a-bungarotoxin-binding regions on the extracellular part of the a-chain of Torpedo california acetylcholine receptor. Biochem. J. 248: 847–852.

    Google Scholar 

  • Obara, K., Fuse, N., Tsuchiya, T., Nonomura, Y, Menez, A. and Tamiya, T. (1989) Sequence analysis of a cDNA encoding a erabutoxin b from the sea-snake Laticauda semifasciata. Nucleic Acids Res. 17, 10490.

    Article  PubMed  CAS  Google Scholar 

  • Ruan, K.H., Spurlino, J., Quiocho, F.A. and Atassi, M.Z. (1990) Acetylcholine receptor-a-bungarotoxin interactions: Determination of the region-to-region contacts by peptide-peptide interactions and molecular modeling of the receptor cavity. Proc. Natl. Acad. Sci. USA 87: 6156–6160.

    Article  PubMed  CAS  Google Scholar 

  • Ruan, K.H., Stiles, B.G. and Atassi, M.Z. (1991) The short-neurotoxin-binding regions on the a-chain of human and Torpedo californica acetylcholine receptors. Biochem. J. 214: 849–854.

    Google Scholar 

  • Sanger, F., Nicklen, S. and Coulson, A.R. (1977) DNA sequencing with chain–terminating inhibitors, Proc. Natl. Acad. Sci. USA 74: 5463–5467.

    Article  PubMed  CAS  Google Scholar 

  • Tamiya, N., Lamouroux, A., Julien, J.F., Grima, B., Mallet, J., Fromageot, P. and Menez, A. (1985) Cloning and sequence analysis of the cDNA encoding a snake neurotoxin precursor. Biochimie 67: 185–189.

    Article  PubMed  CAS  Google Scholar 

  • Tsernoglou, D. and Petsko, G. A. (1976) The crystal structure of a postsynaptic neurotoxin from sea snake at 2.2 A resolution. FEBS Lett. 68: 1–4.

    Article  PubMed  CAS  Google Scholar 

  • Walkinshaw, M. D., Saenger, W. and Maelicke, A. (1980) Three-dimensional structure of the long neurotoxin from cobra venom. Proc. Natl. Acad. Sci. USA 11: 2400–2404.

    Article  Google Scholar 

  • Wu, S. H., Chen, C. J., Tseng, M. J. and Wang, K. T. (1983) The modification of a-bungarotoxin by digestion with trypsin. Arch. Biochem. Biophys. 227: 111–117.

    CAS  Google Scholar 

  • Yang, C. C. (1964) Purification of toxic proteins from cobra venom. J. Formosan Med. Assoc. 63: 325–331.

    CAS  Google Scholar 

  • Yang, C. C. (1965) Crystallization and properties of cobrotoxin from Formosan cobra venom. J. Biol. Chem. 240: 1616–1618.

    PubMed  CAS  Google Scholar 

  • Yang, C. C. (1967) The disulfide bonds of cobrotoxin and their relationship to lethality. Biochim. Biophys. Acta 133: 346–355.

    CAS  Google Scholar 

  • Yang, C. C. (1974) Chemistry and evolution of toxins in snake venoms. Toxicon 12: 1–43.

    Article  PubMed  CAS  Google Scholar 

  • Yang, C. C. (1984) Snake neurotoxin. The Snake 16: 90–103.

    CAS  Google Scholar 

  • Yang, C. C. (1987) Cobrotoxin structure and function, in “Pharmacology” (Rand, M. J. and Raper, C, eds.) Elsevier Biomedical Division, Amsterdam, pp. 871–874.

    Google Scholar 

  • Yang, C.C. (1988) Chemistry and immunochemistry of cobrotoxin. J. Chin. Biochem. Soc. 17: 20–31.

    CAS  Google Scholar 

  • Yang, C.C. (1992) Chemistry of snake neurotoxins and future perspective. J. Chin. Chem. Soc. 39: 731–740.

    CAS  Google Scholar 

  • Yang, C.C. (1993) Structure and function of snake neurotoxin, in “Recent Advances in Molecular and Biochemical Research on Protein” ( Wei, Y.H., Chen, CS. and Su, J.C, eds.) World Scientific, Singapore, pp. 105–118.

    Google Scholar 

  • Yang, C. C, Chang, C. C. and Liou, I. F. (1974) Studies on the status of arginine residues in cobrotoxin. Biochim. Biophys. Acta 365: 1–14.

    CAS  Google Scholar 

  • Yang, C. C., King, K. and Sun, T. P. (1981) Chemical modification of lysine and histidine residues in phospholipase A2 from the venom of Naja naja atra (Taiwan cobra). Toxicon 19: 645–659.

    Article  PubMed  CAS  Google Scholar 

  • Yang, C. C., Yang, H. J. and Chiu, R. H. C. (1970) The position of disulfide bonds in cobrotoxin. Biochim. Biophys. Acta 214: 355–363.

    PubMed  CAS  Google Scholar 

  • Yang, C. C., Yang, H. J. and Huang, J. S. (1969) The amino acid sequence of cobrotoxin. Biochim. Biophys. Acta 188: 65–67.

    PubMed  CAS  Google Scholar 

  • Yu, C., Bhaskaran, R., Chuang, L. C. and Yang, C. C. (1993) Solution conformation of cobrotoxin: A nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study. Biochemistry 32: 2131–2136.

    Article  PubMed  CAS  Google Scholar 

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Authors and Affiliations

  1. Institute of Life Sciences, National Tsing Hua University, Hsinchu, 30043, Taiwan, Republic of China

    C. C. Yang

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  1. C. C. Yang
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Editors and Affiliations

  1. University of Massachusetts, Dartmouth, North Dartmouth, Massachusetts, USA

    Bal Ram Singh

  2. Colorado State University, Fort Collins, Colorado, USA

    Anthony T. Tu

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© 1996 Plenum Press, New York

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Yang, C.C. (1996). Structure and Function of Cobra Neurotoxin. In: Singh, B.R., Tu, A.T. (eds) Natural Toxins 2. Advances in Experimental Medicine and Biology, vol 391. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0361-9_5

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  • DOI: https://doi.org/10.1007/978-1-4613-0361-9_5

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-8016-0

  • Online ISBN: 978-1-4613-0361-9

  • eBook Packages: Springer Book Archive

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