Effect of pH on the conformation, interaction with membranes and hemolytic activity of sticholysin II, a pore forming cytolysin from the sea anemone Stichodactyla helianthus

Toxicon

Volumn 39, Issue 4, 2001, Pages 539-553

  Alvarez, Carlos ^a   Pazos, Isabel F ^a   Lanio, Maria E ^a   Martinez, Diana ^a   Schreier, Shirley ^b   Casallanovo, F ^b   Campos, Ana Maria ^c   Lissi, Eduardo ^c  

^a UNIVERSITY OF HAVANA   (Cuba)

^b UNIVERSITY OF SÃO PAULO   (Brazil)

^c UNIVERSIDAD DE SANTIAGO DE CHILE   (Chile)

Author keywords

Conformational changes; Hemolytic activity; Membrane binding; pH; Sticholysin II

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; CYTOLYSIN; DYE; LIPOSOME; PHOSPHATIDYLCHOLINE; PRODAN; SEA ANEMONE TOXIN; SPHINGOMYELIN; STICHOLYSIN II; UNCLASSIFIED DRUG;

ARTICLE; ARTIFICIAL MEMBRANE; CHANNEL GATING; CIRCULAR DICHROISM; CONTROLLED STUDY; ERYTHROCYTE; ERYTHROCYTE MEMBRANE; FLUORESCENCE; HEMOLYSIS; HUMAN; HUMAN CELL; MEMBRANE BINDING; PH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; SEA ANEMONE; STICHODACTYLA HELIANTHUS;

EID: 0342844373     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0041-0101(00)00166-5     Document Type: Article

References (34)

1. Alvarez C., Lanio M.E., Tejuca M., Martínez D., Pazos F., Campos A.M., Encinas M.V., Pertinhez T., Schreier S., Lissi E.A. The role of ionic strength on the enhancement of the hemolytic activity of Sticholysin I, a cytolysin from Stichodactyla helianthus. Toxicon. 36:(1):1998;165-178.
2. Belmonte G., Pederzolli C., Macek P.y., Menestrina G. Pore formation by the sea anemone Cytolysin equinatoxin II in red blood cells and model lipid membranes. J. Membrane Biol. 131:1993;11-22.
3. Campos A.M., Lissi E.A., Vergara C., Lanio M.E., Alvarez C., Pazos I., Morera V., Garcia I.y., Martinez D. Kinetics and mechanism of St I modification by peroxyl radicals. J. Protein. Chem. 18:1999;297-306.
4. Dathe M., Schümann M., Wieprecht T., Winkler A., Beyermann M., Krause E., Matusuzaki K., Murase O., Bienert M. Biochemistry. 35:1996;12612-12622.
5. De los Ríos V., Mancheño J.M., Lanio M.E, Oñaderra M., Gavilanes J. Mechanism of the leakage induced on lipid model membranes by the hemolytic protein Sticholysin II from the sea anemone Stichodactyla helianthus. Eur. J. Biochem. 252:1998;284-289.
6. Doyle J.W., Kem W.R., Vilallonga F.A. Interfacial activity of an ion channel-generating protein cytolysin from the sea anemone Stichodactyla helianthus. Toxicon. 27:1989;465-471.
7. Gómez T., Romero D.L., Wong L., Barral A.M., Martínez J.R., Chávez M.A. Isolation and partial purification of two toxins and a protease inhibitor from Stoichactis helianthus anemone. Rev. Cubana Invest. Biom. 5:1986;117-125.
8. Greene F.C. Interactions of anionic and cationic fluorescent probes with proteins: the effect of charge. J. Protein Chem. 3:1984;167-179.
9. Haskad C.A., Li-Chan E.C.Y. Hydrophobicity of bovine serum albumin and ovalbumin determined using uncharged (PRODAN) and anionic (ANS) fluorescent probes. J. Agric. Food Chem. 46:1998;2671-2677.
10. Kem W.R., Dunn B.M. Separation and characterisation of four different amino acid sequence variants of a sea anemone protein cytolysin. Toxicon. 26:1988;997-1008.
11. Khoo H.E., Fong Ch.L., Yuen R., Chen D. Stimulation of haemolytic activity of sea anemone cytolysins by 8-anilino-1-naphthalenesulphonate. Biochem. Biophys. Res. Comm. 232:1997;422-426.
12. Lakowicz J.R. Principles of Fluorescence Spectroscopy. 1983;Plenum Press, New York.
13. Lanio, M.E. Morera, V. Alvarez, C. Tejuca, M. Gomez, T. Pazos, F. Besada, V. Martinez, D. Huerta, V. Padron, G., Chavez, M.A., 1999. Purification and characterization of two hemolysins from Stichodactyla helianthus. Toxicon, submitted.
14. Macek P., Belmonte G., Pederzolli C., Dalla-Serra M., Menestrina G. Intrinsic tryptophan fluorescence of equinatoxin II, a pore-forming polypeptide from the sea anemone Actinia equina L. monitors its interaction with lipid membranes. Eur. J. Biochem. 234:1995;329-335.
15. Macek P., Lebez D. Isolation and characterization of three lethal and hemolytic toxins from the sea anemone Actinia equina L. Toxicon. 26:1988;441-451.
16. Malavasic M., Poklar N., Macek P., Vesanver G. Fluorescence studies of the effect of pH, guanidine hydrochloride and urea on equinatoxin II conformation. Biophys. Biochim. Acta. 1280:1996;65-72.
17. Matulis D., Lovrien R. 1-Anilino-8-naphthalene sulfonate anion-protein binding depends primarily on ion pair formation. Biophys. J. 74:1998;422-429.
18. Menestrina G., Tejuca M. Secondary structure of sea anemone cytolysins in soluble and membrane bound form by infrared spectroscopy. Biochem. Biophys. Res. Commun. 254:1999;174-180.
19. Morera V., Gomez T., Besada V., Estrada R., Pons T., Alvarez C., Tejuca M., Lanio M.E., Pazos F. Primary structure analysis of the hemolytic polypeptide sticholysin isolated from a sea anemone. Advances in Modern Biotechnology. 2:1994;135.
20. Nordera P., Dalla Serra M., Menestrina G. The adsorption of pseudomonas aeruginosa exotoxin A to phospholipid monolayers is controlled by pH and surface potential. Biophys. J. 73:1997;1468-1478.
21. Ostaloza H., Bakas L., Goñi F.M. Balance of electrostatic and hydrophobic interactions in the lysis of model membranes by E. coli α-haemolysin. J. Membrane Biol. 158:1997;137-145.
22. Parker M.W., Pattus P. Rendering a membrane protein soluble in water: a common packing motif in bacterial protein toxins. Trends Biochem. Sci. 18:1993;391-395.
23. Pazos I.F., Alvarez C., Lanio M.E., Martínez D., Morera V., Lissi E., Campos A.M. Modification of sticholysin II hemolytic activity by free radicals. Toxicon. 36:(10):1998;1383-1393.
24. Poklar N., Lah J., Salobir M., Macek P., Vesnaver G. pH and temperature-induced molten globule-like denatures states of equinatoxin II: a study by UV-melting, DSC, far and near-UV CD spectroscopy, and ANS fluorescence. Biochemistry. 36:1997;14345-14352.
25. Tejuca M., Dalla Serra M., Ferreras M., Lanio M.E, Menestrina G. Mechanism of membrane permeabilization by sticholysin I, a cytolysin isolated from the venom of the sea anemone Stichodactyla helianthus. Biochemistry. 35:1996;14947-14957.
26. Tejuca M., Luzardo M.C., Alvarez C., Veitía R., Pazos F., Lanio M.E. Influence of pH on the mechanism of a cytolysin of Stichodactyla helianthus. Rev. Biologia. 10:1994;125.
27. Tsou Ch-L. Inactivation precedes overall molecular conformation changes during enzyme denaturation. Biochim. Biophys. Acta. 1253:1995;151-162.
28. Turk T. Cytolytic toxins from sea anemones. J. Toxicol. Toxin Rev. 10:1991;223-262.
29. Turk T., Macek P., Gubensek F. Chemical modification of equinatoxin II, a lethal and cytolytic toxin from the sea anemone Actinia equina. Toxicon. 27:1989;375-384.
30. Turk T., Macek P., Gubensek F. The role of tryptophan in structural and functional properties of equinatoxin II. Biochim. Biophys. Acta. 1119:1992;1-5.
31. Uversky V.N., Winter S., Löber G. Use of fluorescence decay times of 8-ANS-protein complexes to study the conformational transitions in proteins which unfold through the molten globule state. Biophys. Chem. 60:1996;79-88.
32. Van der Goot F.G., Gonzalez Mañas, J.N., Lakey J.H., Pattus F. A "molten globule" membrane-insertion intermediate of pore-forming domain of colicin A. Nature. 354:1991;408-410.
33. Weber G., Farris F.J. Synthesis and spectral properties of a hydrophobic fluorescent probe: 6-propionyl-2-(dimethylamino)naphthalene. Biochemistry. 18:1979;3075-3078.
34. Zakharov S.D., Heymann J.B., Shang Y.-L., Cramer W.A. Membrane binding of the colicin E1 channel: activity requires an electrostatic interaction of intermediate magnitude. Biophys. J. 70:1996;2774-2783.