Chemical modification of methionines in a cobra venom cytotoxin differentiates between lytic and binding domains

Toxicology and Applied Pharmacology

Volumn 139, Issue 2, 1996, Pages 234-242

  Stevens Truss, Regina ^a,b   Hinman, Channing L ^a  

^a MEDICAL COLLEGE OF OHIO   (United States)

^b UNIVERSITY OF MICHIGAN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COBROTOXIN;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; CELL TYPE; CHEMICAL MODIFICATION; CONTROLLED STUDY; CYTOTOXICITY; DRUG BINDING; HEART MUSCLE CELL; HUMAN; HUMAN CELL; NONHUMAN; OXIDATION; PROTEIN MODIFICATION; RAT; T LYMPHOCYTE;

ANIMALIA; ATRA; NAJA ATRA; NAJA NAJA;

EID: 0030221106     PISSN: 0041008X     EISSN: None     Source Type: Journal    
DOI: 10.1006/taap.1996.0162     Document Type: Article

References (41)

1. 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.
2. Borkow, G., Chaim-Matyas, A., and Ovadia, M. (1991). Effect of iodination on the activity of cytotoxin P4 of Naja nigricollis nigricollis. Biochem. Int. 25, 261-269.
3. II1 from Naja melanoleuca venom. Biochim. Biophys. Acta 534, 322-330.
4. Carlsson, F. H. H. (1980). The preparation of 3-nitrotyrosyl derivatives of three elapid venom cardiotoxins. Biochim. Biophys. Acta 624, 460-472.
5. Carlsson, F. H. H. (1987). The selective S-alkylation of a methionine residue in an elapid venom cardiotoxin. Int. J. Biochem. 19, 915-921.
6. Carlsson, F. H. H., and Louw, A. I. (1987). Properties of some 3-nitrotyrosyl elapid venom cardiotoxins. Int. J. Biochem. 19, 9-16.
7. Chaim-Matyas, A., Borkow, G., and Ovadia, M. (1991). Isolation and characterization of a cytotoxin P4 from the venom of Naja nigricollis nigricollis preferentially active on tumor cells. Biochem. Int. 24, 415-421.
8. Chen, Y. H., Hu, C. T., and Yang, J. T. (1984). Membrane disintegration and hemolysis of human erythrocytes by snake venom cardiotoxin (a membrane-disruptive polypeptide). Biochem. Int. 8, 329-338.
9. Dufton, M. J., and Hider, R. C. (1988). Structure and pharmacology of elapid cytotoxins. Pharmacol. Ther. 36, 1-40.
10. Dufton, M. J., and Hider, R. C. (1991). The structure and pharmacology of elapid cytotoxins. In Snake Toxins (A. L. Harvey, Ed.), pp. 259-302. Pergamon, New York.
11. Fishman, A., Bar-Kana, Y., Steinberger, I., and Lorberboum-Galski, H. (1994). Increased cytotoxicity of interleukin 2-pseudomonas exotoxin (IL2-PE) chimeric proteins containing a targeting signal for lysosomal membranes. Biochemistry 33, 6235-6243.
12. Gatineau, E., Toma, F., Montenay-Garestier, Th., Takechi, M., Fromageot, P., and Menez, A. (1987). Role of tyrosine and tryptophan residues in the structure-activity relationships of a cardiotoxin from Naja nigricollis venom. Biochemistry 26, 8046-8055.
13. Gatineau, E., Takechi, M., Bouet, F., Mansuelle, P., Rochat, H., Harvey, A. L., Montenay-Garestier, Th., and Menez, A. (1990). Delineation of the functional site of a snake venom cardiotoxin: Preparation, structure, and function of monoacetylated derivatives. Biochemistry 29, 6480-6489.
14. Gilquin, B., Roumestand, C., Zinn-Justin, S., Menez, A., and Toma, F. (1993). Refined 3-dimensional solution structure of a snake cardiotoxin: Analysis of the side-chain organization suggests the existence of a possible phospholipid binding site. Biopolymers 33, 1659-1675.
15. Gross, E., and Witkop, B. (1962). Nonenzymatic cleavage of peptide bonds: the methionine residues in bovine pancreatic ribonuclease. J. Biol. Chem. 237, 1856-1860.
16. Hansen, M. B., Nielsen, S. E., and Berg, K. (1989). Re-examination and further development of a precise and rapid dye method for measuring cell growth/cell kill. J. Immunol. Methods 119, 203-210.
17. Harvey, A. L. (1985). Cardiotoxins from cobra venoms: Possible mechanisms of action. Toxicol. Toxin Rev. 4, 41-69.
18. Harvey, A. L. (1991). Cardiotoxins from cobra venoms. In Handbook of Natural Toxins, Vol. 5, Reptile and Amphibian Venoms (A. T. Tu, Ed.), pp. 85-106. Dekker, New York.
19. Harvey, A. L., Marshall, R. J., and Karlsson, E. (1982). Effects of purified cardiotoxins from the Thailand cobra [Naja naja siamensis] on isolated skeletal and cardiac muscle preparations. Toxicon 20, 379-396.
20. Hinkle, D. E., Wiersma, W., and Jurs, S. G. (1988). Applied Statistics for the Behavioral Sciences, 2nd ed. Houghton Mifflin Co., Boston.
21. Hinman, C. L., Jiang, X. L., and Tang, H.-P. (1990). Selective cytolysis by a protein toxin as a consequence of direct interaction with the lymphocyte plasma membrane. Toxicol. Appl. Pharmacol. 104, 290-300.
22. Hodges, S. J., Agbaji, A. S., Harvey, A. L., and Hider, R. C. (1987). Cobra cardiotoxins: Purification, effects on skeletal muscle and structure/activity relationship. Eur. J. Biochem. 165, 373-383.
23. Hung, M. C., Cheng, K. L., and Lai, M. Z. (1977). Studies on the status of the Met-Phe-Met segment and disulfide linkages in Formosan cobra cardiotoxin. J. Chin. Biochem. Soc. 6, 27-36.
24. Karlsson, E., Arnberg, H., and Eaker, D. (1971). Isolation of the principal neurotoxins of two Naja naja subspecies. Eur. J. Biochem. 21, 1-16.
25. Keung, W. M., Leung, W. W., and Kong, Y. C. (1975). Studies on the status of disulfide linkages and tyrosine residues in cardiotoxin. Biochem. Biophys. Res. Commun. 66, 383-392.
26. Kini, R. M., and Evans, H. J. (1989). Role of cationic residues in cytolytic activity: modification of lysine residues in the cardiotoxin from Naja nigricollis venom and correlation between cytolytic and antiplatelet activity. Biochemistry 28, 9209-9215.
27. Lin, S. R., Chang, K. L., and Chang, C. C. (1993). Chemical modification of amino groups in cardiotoxin-III from Taiwan cobra (Naja-naja-atra) venom. Biochem. Mol. Biol. Int. 31, 175-184.
28. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951). Protein measurement with the folin phenol reagent. J. Biol. Chem. 193, 265-275.
29. Markwell, M. A. K. (1982). A new solid-state reagent to iodinate proteins. Anal. Biochem. 125, 427-432.
30. 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. Biochimie 72, 575-588.
31. Nyburg, S. C. (1974) "BMFIT." Acta Crystallogr. B30, 251-253.
32. Rees, B., Samama, J. P., Thierry, J. C., Gilibert, M., Fischer, J., Schweitz, H., Lazdunski, M., and Moras, D. (1987). Crystal structure of a snake venom cardiotoxin. Proc. Natl. Acad. Sci. USA 84, 3132-3136.
33. Shashidharan, P., and Ramachandran, L. K. (1987). Effect of N-bromosuccinimide-modification of tyrosine side chains of cardiotoxin II of the Indian cobra on biological activity. J. Biosci. 11, 287-297.
34. Shechter, Y., Burstein, Y., and Patchornik, A. (1975). Selective oxidation of methionine residues in proteins. Biochemistry 14, 4497-4503.
35. Stevens-Truss, R., Messer, W. S., Jr., and Hinman, C. L. (1996). Heart and T-lymphocyte cell surfaces both exhibit positive cooperativity in binding a membrane-lytic toxin. J. Membr. Biol. 150, 113-122.
36. Suresh-Kumar, T. K., and Ramachandran, L. K. (1990). Effect of modification of tyrosine residues in cytotoxin-1 from Indian cobra venom (Naja naja naja). Biochem. Int. 20, 879-885.
37. Tripos Associates (1991). Sybyl, version 5.5C. St. Louis, MO.
38. Weiner, P. K., and Kollman, P. A. (1981) AMBER: Assisted Model Building with Energy Refinement. A general program for modeling molecules and their interactions. J. Comp. Chem. 2, 287-303.
39. Wong, C. H., Chen, Y. H., Hung, M. C., and Wang, K. T. (1978). Renaturation of a reduced Taiwan cobra cardiotoxin. Biochim. Biophys. Acta 533, 105-111.
40. Wong, C. H., Ho, C. L., and Wang, K. T. (1980). The status of methionine in cobra cardiotoxin. J. Chin. Biochem. Soc. 9, 25-29.
41. Zusman, N., Cafmeyer, N., and Hudson, R. A. (1981). Purification and characterization of the cardiotoxins from the venom of the Thailand cobra, Naja naja siamensis. Comp. Biochem. Physiol. B 69, 345-351.