A case study of cardiotoxin III from the Taiwan cobra (Naja naja atra): Solution structure and other physical properties

Advances in Experimental Medicine and Biology

Volumn 391, Issue , 1996, Pages 115-129

  Kumar, T K S ^a   Lee, C S ^a   Yu, C ^a  

^a NATIONAL TSING HUA UNIVERSITY   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

CARDIOTOXIN; COBROTOXIN; SNAKE VENOM;

AMINO ACID SEQUENCE; ARTICLE; CARDIOTOXICITY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN ISOLATION; SEQUENCE HOMOLOGY; SNAKEBITE;

EID: 0029950894     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4613-0361-9_7     Document Type: Article

References (102)

1. Dufton, M. J., and Hider, R. C., 1991, in Snake toxins, Harvey, A.L., Ed., Pergamon Press, New York, pp 259-298.
2. Harvey, A.L., 1991, Cardiotoxins from snake venoms. In Handbook of Natural toxins, Tu, A.T., Ed., Marcel Dekker, New York, Vol 5, pp 85-106.
3. Dufton, M.J., and Hider, R.C., 1988, Structure and pharmacology of Elapid cytotoxins, Pharmacol. Ther. 36:1-40.
4. Harvey, A.L., 1985, Cardiotoxins from cobra venoms: possible mechanisms of action, Toxicol. Toxin. Rev. 4:41-69.
5. Menez, A., Botems, F., Roumestand, C., Gilquin, B., and Toma, F., 1992, Structural basis for functional diversity of animal toxins, Proc. Roy. Soc. Edinburgh 90B: 83-103.
6. Rees, B., and Bilwes, A., 1993, Three-dimensional structures of neurotoxins and cardiotoxins, Chem. Res. Toxicol. 6: 385-406.
7. Dufton, M.J., and Hider, R.C., 1983. Conformational properties of the neurotoxins and cytotoxins isolated from Elapid snake toxin. CRC Crit. Rev. Biochem. 114: 113-114.
8. Yu, C., Bhaskaran, R., and Yang, C.C., 1994, Structures in solution of toxins from Taiwan cobra, Naja naja atra, derived from NMR spectra, J. Toxin. Toxicol. Rev. 13: 291-315.
9. Basus, V.J., Song, G., and Hawrot, E., 1993, NMR solution structure of an α-bungarotoxin nicotinic peptide complex. Biochemistry 32: 12290-12298.
10. Conti-Tronconi, B.M., Tang, F., Diethelm, B.M., Wu, X., Tang, F., Beratazzon, T., Schroder, B., Reinhardt-Maeclicke, S., and Maelicke, A., 1991, α-bungarotoxin and the competing antibody Wf6 interact with different amino acids within the same cholinergic subsite, Biochemistry 30: 2575-2584.
11. Traztos, S.J., and Remoundos, M.S., 1990, Fine localisation of the major α-bungarotoxin binding-site to residues-α 189-195 of the torpedo acetylcholine receptor residues-189, residues-190, and residues-195 are indispensible for binding, J. Biol. Chem. 265: 21462-21467.
12. Radding, W., Corfield, P.W.R., Levinson, L.S., Hashim, G.A., and Low, B.W., 1988, Alpha-toxin binding to acetylcholine receptor 179-191 peptides - Intrinsic fluorescence studies, FEBS Lett. 231: 212-216.
13. Fletcher, J.P., and Jiang, M.-S., 1993, Possible mechanisms of action of cobra snake venom cardiotoxins and bee venom mellitin, Toxicon, 31: 695-699.
14. Grognet, J.M., Menez, A., Drake, A., Hayashi, K., Morrison, I.E.G., and Hider, R.C., 1988, Circular dichroic spectra of Elapid cardiotoxins, Eur. J. Biochem. 172: 383-388.
15. Kini, R.M., and Evans, H.J., 1988, Mechanism of platelet effects of cardiotoxins from Naja nigricollis crawshawii (spitting cobra) snake venom, Thromb. Res. 52: 185-195.
16. Hinman, C.L., Lepisto, E., Stevens, R., Mongomery, I.N., Rauch, H.C., and Hudson, R.A., 1987, Effects of cardiotoxin D from Naja Siamensis snake venom upon murine splenic lymphocytes, Toxicon 25: 1011-1014.
17. Takechi, M., Tanaka, Y., and Hayashi, K., 1986, Binding of cardiotoxin analogue III from Formosan cobra to FL cells Le, FEBS Lett. 205:143-146.
18. Gatineau, E., Takeshi, M., Bowet, F., Mansuelle, P., Rochat, H., Harvey, A.L., Montenay-Garestier, T., and Menez, A., 1990, Delineation of the functional site of a snake venom cardiotoxin : preparation, structure, and function of monoacetylated derivatives, Boichemistry 29: 6480-6489.
19. Kini, R.M., and Evans, H.J., 1989, Role of cationic residues in cytolytic activity : modification from Naja nigricollis and correlation between cytolytic and anti-platelet effect, Biochemistry 28: 295-301.
20. Vincent, J.P., Balerna, M. and Lazdunski, M., 1978, Properties of association of cardiotoxin with lipid vesicles and natural membranes : a case study, FEBS Lett. 85: 103-108.
21. Defourcq, J., and Faucon, J.F., 1978, Specific binding of a cardiotoxin from Naja mossambica mosambica to charged phospholipids detected by intrinsic fluorescence, Biochemistry 17: 1170-1176.
22. Batenby, A.M., Bougis, P.E., Rochat, H., Verkleij, A.J., and de Kruijff, B., 1985, Penetration of a cardiotoxin into cardiolipin model membranes and its implications on lipid organisation. Biochemistry 24: 7101-7110.
23. Defourcq, J., Faucon, J.F., Bernard, E., Pezolot, M., Tessier, M., Bougis, P., Rietschoten, J., Delori, P., and Rochat, H., 1982, Structure-function relationships for the cardiotoxins interacting with phospholipids, Toxicon 20: 165-174.
24. Rothman, J.E., and Lenard, J., 1977, Membrane asymmetry, Science 195: 743-753.
25. Desormeaux, A., Laroche, G., Bougis, P.E., and Pezolot, M., 1992, Characterisation by infrared spectroscopy of the interaction of a cardiotoxin with phosphatidic acid and with binary mixtures of phosphatidic acid and phosphatidyl choline, Biochemistry 31: 12173-12182.
26. Bougis, P.E., Tessier, M., Rietschoten, J.V., Rochat, H., Faucon, J.F., and Dufourcq, J., 1983, Are interactions with phospholipids responsible for pharmacological activities of cardiotoxins?, Mol. Cell. Biochem. 55: 49-64.
27. Knowden, M.J., Vitale, A.J., Trumble, M.J., Wesson, C.R., and Trumble, W.R., 1992, A bioassay for cobra cardiotoxin activity using semi-isolated cockroach heart, Toxicon 30: 295-301.
28. Chiou, S., Raynor, R.L., Zheng, B., Chambers, T.C., and Kuo, J.F., 1993, Cobra venom cardiotoxin (cytotoxin) isoforms and neurotoxin : Comparitive potency of protein kinase C inhibition and cancer cell cytotoxicity and modes of enzyme inhibition, Biochemistry 32: 2062-2067.
29. +2 dependent protein kinase, FEBS Lett. 153: 183-186.
30. O'Connell, J.F., Bougis, P.E., and Wuthrich, K., 1993, Determination of the NMR solution structure of cardiotoxin CTX IIb from Naja mossambica mossambica. Eur. J. Biochem. 213: 891-900.
31. Gilquin, B., Roumestand, C., Zinn-Justin, S., Menez, A., and Toma, F., 1993, Refined three-dimensional solution structure of snake cardiotoxin : analysis of the side-chain organization suggests the existence of a possible phospholipid binding site, Biopolymers, 33: 1659-1675.
32. Bhaskaran, R., Huang, C.C., Chang, D.K., and Yu, C., 1994, Cardiotoxin III from the Taiwan cobra (Naja naja atra) : Determination of structure in solution and comparison with short neurotoxins, J. Mol. Biol. 235, 1291-1301.
33. Jahnke, W., Mier, D.F., Beress, L. and Kesseler, H., 1994, Structure of cobra cardiotoxin, CTX I, as derived from Nuclear Magnetic Resonance Spectroscopy and Distance geometry calculations, J. Mol. Biol., 240, 445-458.
34. Bhaskaran, R., Haung, C.C., Tsai, Y.-C., Jayaraman, G., Chang, D.-K., and Yu, C., 1994, Cardiotoxin II from Taiwan cobra venom, Naja naja atra, Structure in solution and comparison among homologous cardiotoxins, J. Biol. Chem., 269: 23500-23508.
35. II1 4 from Naja mossambica mossambica : the refined crystal structure, J. Mol. Biol. 214: 281-297.
36. 0 of Toxin γ, a cardiotoxin from Naja nigricollis venom : Crystal packing reveals a model for insertion into membranes, J. Mol. Biol. 239: 122-136.
37. Yang, C.C., 1974, Chemistry and evolution of toxins in snake venoms, Toxicon 12 : 1-43.
38. Chiou, S.H., Lee, B.S., and Yu, N.T., 1992. Structural analysis and comparison of cobrotoxin and cardiotoxins by near-IR Fourier transform Raman spectroscopy, Biochem. Intl. 274: 747-758.
39. Kumar, T.K.S., Radha, R., and Rambhav, S., What's in a name, Toxicon, 28: 135-138.
40. Yang, C.C., King, K., and Sun, T.P., 1981. Chemical modification of lysine and histidine residues in phospholipase A from the venom of Naja naja atra (Taiwan cobra), Toxicon 19: 645-659.
41. Hayashi, K., Takechi, M., Kaneda, N., and Sasaki, T., 1976, Amino acid sequence of cardiotoxin from the venom of Naja naja atra, FEBS Lett. 66: 210-214.
42. Drake, A.F., Dufton, M.J., and Hider, R.C., (1980). Circular dichroism of Elapid protein toxins, Eur. J. Biochem., 105: 623-628.
43. Hung, M.C., and Chen, Y.H., 1977, Conformational stabilty of a snake cardiotoxin, Int.J.Peptide.Protein Res. 10, 277-289.
44. Dufton, M.J., and Hider, R.C., 1977, Snake toxin secondary structure predictions, J.Mol.Biol., 115, 117-142.
45. Menez, A., Langlet, G., Tamiya, N., and Formagoet, P., 1978, Conformation of snake toxic polypeptides studied by a method of prediction and circular dichroism, Biochemie. 60, 505-513.
46. II 1 from Naja melanoleuca venom, Biochim.Biophys.Acta, 534, 325-329.
47. Gatineau, E., Toma, F., Montenay-Garestier, T., Takechi, M., Fromageot, P., and Menez, A., 1987, The role of tyrosine and tryptophan residues in the structure-activity relationships of a cardiotoxin from Naja nigricollis venom, Biochemistry 26: 8046-8055.
48. Fryklund, L., and Eaker, D., 1975, The complete structure of a cardiotoxin from the venom of Naja nigricollis (African black-necked spitting cobra )Biochemistry, 14: 2865-2871.
49. Menez, A., Gatineau, E., Roumestand, C., Harvey, A.L., Mouawad, L., Gilquin, B., and Toma, F., 1990, Do cardiotoxins possess a functional site - Structural and chemical modification studies reveal the functional site of the cardiotoxin from Naja nigricollis, Biochemie 72: 575-588.
50. Hung, M.C., Pau, Y.H., Cheng, K.L., and Chen, Y.H., 1978, The status of tyrosyl residues in Foromasn cobra cardiotoxin, Biochim.Biophys.Acta 535: 178-182.
51. Louw, A.I., and Visser, L., 1977, Kinetics of lysis by snake venom cardiotoxins, Biochim.Biophys.Acta 498: 143-153.
52. Surewicz, W.K., Stepanik, T.M., Szabo, A.G., Mantsch, H.H., 1988, Lipid induced changes in the secondary structure of snake venom cardiotoxins, J. Biol. Chem. 263: 786-790.
53. Roumestand, C., Gatineau, E., Gilquin, B., Menez, A., and Toma, F., 1990, in Peptides: Chemistry, Structure and Biology, Rivier, J.F. and Marshall, G.R., Eds. Escom, London, pp 622-624.
54. Chiou, S.H., Hung, C.C., Huang, H.C., Chen, S.T., Wang, K.T., and Yang, C.C., 1995, Cardiotoxins and cobrotoxins isolated from Taiwan cobra, Biochem.Biophys.Res.Commun., 206: 22-32.
55. Wuthrich., K., 1990, Protein structure determination in solution by NMR spectroscopy, J. Biol. Chem. 265: 2059-2062.
56. Bhaskaran, R., Yu, C., and Yang, C.C., 1994, Solution structures and functional implications of the toxins from Taiwan cobra venom. J. Protein Chem. 13: 503-504.
57. Kumar, T.K.S., Jayaraman, G., Lee, C.S., Sivaraman, T., Lin, W.Y., and Yu, C., 1995, Identification of 'molten globule' state in an all β-sheet protein. Biochem.Biophys.Res.Commun., (in press).
58. Bax, A., and Davies, D.G., 1985, MLEV-17 based two-dimensional homonuclear magnetisation transfer spectroscopy, J.Magn.Reson. 65: 355-360.
59. Rance, M., Sorensen, O.W., Bodenhaussen, G., Wagner, G., Ernst, R.R., and Wuthrich, K., 1983. Improved spectral resolution in COSY proton NMR spectra of proteins via double quantum filtering, Biochem. Biophys. Res. Commun. 117: 479-485.
60. Marion, D., and Wuthrich, K., 1983. Application of phase sensitive two-dimensional spectroscopy (COSY) for measurements of proton-proton spin-spin coupling constants in proteins, Biochem. Biophys. Res. Commun. 113: 967-974.
61. Kumar, A., Ernst, R.R., and Wuthrich, K., 1980, A two dimensional nuclear overhauser enhancement (2D NOE) experiment for elucidation of complete proton-proton cross-relaxation networks in biological macromolecules, Biochem. Biophys. Res. Commun. 95: 1-6.
62. Wuthrich, K., 1986, NMR of Proteins and Nucleic acids, Wiley, New York.
63. 1H-NMR spectra of proteins, Biochemistry 26: 5953-5958.
64. Gippert, G.P., Yip, P.F., Wright, P.E., and Case, D.A., 1990, Computational methods for determining protein structures from NMR data, Biochem. Pharmacol. 40: 15-22.
65. Nilges, M., Clore, G.M., and Gronenborn, A.M., 1988, Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry - dynamical simulated annealing calculations. FEBS Lett. 229: 317-329.
66. Brunger, A.T., 1992, X-PLOR software manual version 3.0, Yale university, New Haven, CT.
67. 1H-NMR stereospecific assignments by conformational database searches, Biopolymers 29: 813-822.
68. Brooks, B.R., Bruccoleri, R.E., Olafsen, B.D., States, D.J., Swaminathan, S., and Karplus, M., 1983, CHARMM : a program for minimization and dynamics calculations, J. Comput. Chem. 4: 187-217.
69. Clore, G.M. Robien, M.A., and Gronenborn, A.M., 1993, Exploring the limits of precision of protein structures determined by Nuclear Magnetic Resonance spectroscopy, J. Mol Biol. 231: 82-102.
70. Richardson, J.S., 1981, The anatomy and taxanomy of protein structure, Adv. Protein. Chem. 34: 167-339.
71. Singhal, A.K., Chien, K.Y., Wu, W.G., and Rule, G.S., 1993, Solution structure of cardiotoxin V from Naja naja atra, Biochemistry 32: 8036-8044.
72. Breckenridge, R., and Dufton, M.J., 1987, The structural evolution of cobra venom cytotoxins, J. Mol. Evol. 26: 274-283.
73. Karlsson, E., 1979, Chemistry of protein toxins in snake venoms, In hand book of experimental pharmacology (Lee, C.Y. Eds.) Springer Verlag, Berlin, Vol 52 pp 159-172.
74. Wise, B.C., Chou, C.H.J., Glass, D.B., Katoh, N., Kibler, R.F., Kuo, J.R. Raynor, R.F., Schatzman, R.C., and Turner, R.S., 1982, Phospholipid-sensitive Ca dependent protein kinase from heart, 2. Substrate specificity and inhibition by various agents, J. Biol. Chem. 257: 8489-8495.
75. +2-calmodulin dependent protein kinase-II and synaptosomal membrane Na,K-ATPase and Na pump and differentiation of H 160 cells, J. Biol. Chem. 266: 2753-2758.
76. Lee, C.Y., 1972, Chemistry and pharmacology of polypeptide toxins in snake venoms, Ann. Rev. Pharmacol 12: 265-293.
77. Chien, K.Y., Huang, W.N., Jean, J.H., and Wu, W.G., 1991, Fusion of spingomyelin vesicles induced by proteins from Taiwan cobra (Naja naja atra), J. Biol. Chem. 266: 3232-3259.
78. Chien, K.Y., Chiang, C.M., Hseu, Y.U., Vyas, A.A., Rule, G.S., and Wu, W.G., 1994, Two distinct types of cardiotoxin as revealed by the structure and activity relationship of their interaction with zwitterionic phspholipid dispersions, J. Biol. Chem. 269: 14473-14483.
79. Ksenzhek, O.S., Gerod, V.S., Omel'Chenko, A.M., Semenov, S.N., Sotnichenkov, A.I., and Miroschinikov, A.I., 1978, Interaction of the cardiotoxin of the venom of the cobra Naja naja oxiana with phospholipid membrane model system, Mol. Biol. 12: 1057-1065.
80. Sandblom, J., and Diaz, E., 1984, Cardiotoxin-induced channels in lipid bilayer membranes, Proc.Int.Union. Pure Appl. Biophys (8th Int. Congr.) pp-60.
81. Tanford, C., 1968, Protein denaturation, Adv. Protein. Chem. 23: 121-275.
82. Leroy, E., Mikou, A., Yinshan, Y., and Guittet, E., 1993, NMR solution structure of α-Cobratoxin at pH 3.2 and at pH 7.5, J. Mol. Graphics, 4: 65-70.
83. Barrick, D., Hughson, E.M., and Baldwin, R.L., 1994, Molecular mechanisms of acid denaturation - the role of histidine residues in the partial unfolding of apomyoglobin. J Mol. Biol. 237: 588-601.
84. Hughson, F.M., Wright, P.E., and Baldwin, R.L., 1990. Structural characterisation of a partly folded apomyoglobin intermediate, Science 249: 1544-1548.
85. Kumar, T.K.S., Subbiah, V., Ramakrishna, T., and Pandit, M.W., 1994, Trichloacetic acid - induced unfolding of bovine pancreatic ribonuclease - existence of a molten globule like state, J. Biol.Chem. 269: 12620-12625.
86. Wuthrich, K., 1994, NMR assignments as a basis for structural characterisation of denatured states of globular proteins, Curr. Opin. Struc. Biol. 4: 93-99.
87. Radford, S.R., Dobson, C.M., and Evans, P.A., 1992, The folding of hen lysozyme involves partially structured intermediates and multiple pathways, Nature 358: 302-307.
88. Ballery, N., Desmadril, M., Minard, P., and Yon, J.M., 1993, Characterisation of an intermediate of phosphoglycerate kinase - chemical reactivity of genetically introduced cysteinyl residues during the folding process, Biochemistry 32: 669-678.
89. Ptitsyn, O.B., 1987, Protein folding - hypotheses and experiments. J. Protein. Chem. 6: 273-293.
90. Kuwajima, K., 1989, The molten globule state as a clue for understanding the folding cooperativity of globular protein structure, Proteins:Stuc.Func.Genet. 6: 87-103.
91. Goto, Y., Calciano, L.J., Fink, A.L., 1990, Mechanism of acid induced folding of proteins, Proc. Natl. Acad. Sci. (USA) 87:573-577.
92. Ptitsyn, O.B., and Uversky, V.N., 1994, The molten globule is a third thermodynamical state of protein molecules, FEBS Lett. 341: 15-18.
93. Jaenicke, R., 1991, Protein Folding: Local structures, Domains, Subunits and assemblies, Biochemistry 30: 3161-3169.
94. Ptitsyn, O.B., 1992, in Protein Folding (Creighton, T.E., Eds.) Freeman and Co. New York pp 243-300.
95. Jeng, M.F., and Englander, S.W., 1991, Stable submolecular folding units in a compact form of Cyt-C. J. Mol. Biol 221: 1045-1061.
96. Marston, F.A.O., 1986, The purification of eucaryotic polypeptides, Biochem. J. 240: 1-12.
97. Goldenberg, D.P., 1992, Native and non-native intermediates in the BPTI folding pathway, Trends Biochem. Sci. 17: 257-261.
98. Weissman, J.S., and Kim, P.S., 1991, Reexamination of the folding pathway of BPTI - predominance of native intermediates, Science 253: 1386-1393.
99. 1H nuclear magnetic resonance of the (5-55) single disulfide folding intermediate of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 222: 373-390.
100. Woodward, C.K., 1994, Hydrogen exchange rates and protein folding, Curr. Opin. Struc. Biol. 4: 112-116.
101. Briggs, M., and Roder, H., 1992, Early hydrogen-bonding events in the folding reaction of ubiquitin, Proc. Natl. Acad. Sci. (USA) 89: 2017-2021.
102. Udgaonker, J., and Baldwin, R.L., 1990, Early folding intermediate of ribonucease A, Proc. Natl. Acad. Sci. (USA) 87: 8197-8201.