Characterization of the interaction of hemolytic lectin CEL-III from the marine invertebrate, Cucumaria echinata, with artificial lipid membranes: Involvement of neutral sphingoglycolipids in the pore-forming process

Journal of Biochemistry

Volumn 125, Issue 2, 1999, Pages 277-284

  Hatakeyama, Tomomitsu ^a   Sato, Taiji ^a   Taira, Etsuyo ^a   Kuwahara, Hiromiki ^a   Niidome, Takuro ^a   Aoyagi, Haruhiko ^a  

^a NAGASAKI UNIVERSITY   (Japan)

Author keywords

Calcium; Cucumaria echinata; Glycolipid; Hemolysin; Lectin

Indexed keywords

CARBOHYDRATE; CARBOXYFLUORESCEIN; GLOBOSIDE; GLYCOSPHINGOLIPID; HORSERADISH PEROXIDASE; LACTOSYLCERAMIDE; LECTIN; LIPOSOME; MEMBRANE LIPID; RECEPTOR;

ARTICLE; CELL VACUOLE; CHANNEL GATING; COLLOID; ELECTRON MICROSCOPY; ERYTHROCYTE MEMBRANE; HEMOLYSIS; INVERTEBRATE; LECTIN BINDING; LIPID MEMBRANE; NONHUMAN; OLIGOMERIZATION; OSMOTIC FRAGILITY; RUPTURE; TEMPERATURE;

EID: 0033032077     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022284     Document Type: Article

References (29)

1. +-dependent lectins form the marine invertebrate, Cucumaria echinata. J. Biochem. 116, 209-214
2. Oda, T., Tsuru, M., Hatakeyama, T., Nagatomo, H., Muramatsu, T., and Yamasaki, N. (1997) Temperature-and pH-dependent cytotoxic effect of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata on various cell lines. J. Biochem. 121, 560-567
3. Hatakeyama, T., Nagatomo, H., and Yamasaki, N. (1995) Interaction of the hemolytic lectin CEL-III from the marine invertebrate Cucumaria echinata with the erythrocyte membrane. J. Biol. Chem. 270, 3560-3564
4. Hatakeyama, T., Furukawa, M., Nagatomo, H., Yamasaki, N., and Mori, T. (1996) Oligomerization of the hemolytic lectin CBL-III from the marine invertebrate Cucumaria echinata induced by the binding of carbohydrate ligands. J. Biol. Chem. 271, 16915-16920
5. Hatakeyama, T., Matsuyama, Y., Funada, T., Fukuyama, S., Kuwahara, H., Aoyagi, H., and Yamasaki, N. (1998) Chemical modification of the hemolytic lectin CEL-III by succinic anhydride: Involvement of amino groups in the oligomerization process. Biosci. Biotechnol. Biochem. 62, 1185-1189
6. Fujisawa, T., Kuwahara, H., Hiromasa, Y., Niidome, T., Aoyagi, H., and Hatakeyama, T. (1997) Small-angle X-ray scattering study on CEL-III, a hemolytic lectin from Holothuroidea Cucumaria echinata, and its oligomer induced by the binding of specific carbohydrate. FEBS Lett. 414, 79-83
7. Spangler, D., Heerze, L.D., Clark, C.G., and Armstrong, G.D. (1993) Hydrophobic binding of pertussis toxin is enhanced by oligosaccharide receptors. Arch. Biochem. Biophys. 305, 153-158
8. Hilaire, P.M.S., Boyd, M.K., and Toone, E.J. (1994) Interaction of the Shiga-like toxin type 1 B-subunit with its carbohydrate receptor. Biochemistry 33, 14452-14463
9. Smith, P.K., Krohn, R.I., Hermanson, G.T., Mallia, A.K., Gartner, F.H., Provenzano, M.D., Fujimoto, E.K., Goeke, N.M., Olson, B.J., and Klenke, D.C. (1985) Measurement of protein using bicinchoninic acid. Anal. Biochem. 150, 76-85
10. Nakamura, K. and Handa, S. (1984) Coomassie brilliant blue staining of lipids on thin-layer plates. Anal. Biochem. 142, 406-410
11. 4 (NeuAc) expression in mouse erythrocytes. J. Biochem. 107, 3-7
12. Watanabe, K. and Arao, Y. (1981) A new solvent system for the separation of neutral glycosphingolipids. J. Lipid Res. 22, 1020-1024
13. Tijssen, P. and Kurstak, E. (1984) Highly efficient and simple methods for the preparation of peroxidase and active peroxidase-antibody conjugates for enzyme immunoassays. Anal. Biochem. 136, 451-457
14. Ando, S., Isobe, M., and Nagai, Y. (1976) High performance preparative column chromatography of lipids using a new porous silica, Iatrobeads. I. Separation of molecular species of sphingo-glycolipids. Biochim. Biophys. Acta 424, 98-105
15. Hatakeyama, T., Miyamoto, Y., Nagatomo, H., Sallay, I., and Yamasaki, N. (1997) Carbohydrate-binding properties of the hemolytic lectin CEL-III from the Holothuroidea Cucumaria echinata as analyzed using the carbohydrate-coated microplate. J. Biochem. 121, 63-67
16. Vance, D.E. and Sweeley, C.C. (1967) Quantitative determination of the neutral glyoosyl ceramides in human blood. J. Lipid Res. 8, 621-630
17. Freer, J.H., Arbuthnott, J.P., and Bernheimer, A.W. (1968) Interaction of staphylococcal α-toxin with artificial and natural membranes. J. Bacteriol. 95, 1153-1168
18. Füssle, E., Bhakdi, S., Sziegoleit, A., Traum-Jensen, J., Kranz, T., and Wellensiek, H.-J. (1981) On the mechanism of membrane damage by Staphylococcus aureus α-toxin. J. Cell Biol. 91, 83-94
19. Wilmsen, H.U., Leonard, K.R., Tichelaar, W., Buckley, J.T., and Pattus, F. (1992) The aerolysin membrane channel is formed by heptamerization of the monomer. EMBO J. 11, 2457-2463
20. Cabiaux, V., Buckley, J.T., Wattiez, R., Ruysschaert, J.-M., Parker, M.W., and van der Goot, F.G. (1997) Conformational changes in aerolysin during the transition from the water-soluble protoxin to the membrane channel. Biochemistry 36, 15224-15232
21. Tobkes, N., Wallace, B.A., and Bayley, H. (1985) Secondary structure and assembly mechanism of an oligomeric channel protein. Biochemistry 24, 1915-1920
22. Petosa, C., Collier, R.J., Klimpel, K.R., and van der Goot, F.G. (1997) Crystal structure of the anthrax toxin protective antigen. Nature 385, 833-838
23. 1 ganglioside and related glycolipids. Infect. Immun. 8, 208-214
24. Takamizawa, K., Iwamori, M., Kozaki, S., Sakaguchi, G., Tanaka, R., and Nagai, Y. (1986) TLC immunostaining characterization of Clostridium botulinum type A neurotoxin binding to gangliosides and free fatty acids. FEBS Lett. 201, 229-232
25. Cohen, A., Hannigan, G.E., Williams, B.R.G., and Lingwood, C.A. (1987) Roles of globotriosyl- and galabiosylceramide in verotoxin binding and high affinity interferon receptor. J. Biol. Chem. 262, 17088-17091
26. Shinoda, S., Ishida, K., Oh, E.-G., Sasahara, K., Miyoshi, S., Chowdhury, M.A.R., and Yasuda, T. (1993) Studies on hemolytic action of a hemolysin produced by Vibrio mimicus. Microbiol. Immunol. 37, 405-409
27. Hoch, D.H., Romero-Mira, M., Ehrlich, B.E., Finkelstein, A., Das-Gupta, B.R., and Simpson, L.L. (1985) Channels formed by botulinum, tetanus, and diphtheria toxins in planar lipid bilayers: relevance to translocation of proteins across membranes. Proc. Natl. Acad. Sci. USA 82, 1692-1696
28. Ribi, H.O., Ludwig, D.S., Mercer, K.L., Schoolnik, G.K., and Kornberg, R.D. (1988) Three-dimensional structure of cholera toxin penetrating a lipid membrane. Science 239, 1272-1276
29. Gill, D.M. (1976) The arrangement of subunits in cholera toxin. Biochemistry 15, 1242-1248