Thermostable direct hemolysin of Vibrio parahaemolyticus is a bacterial reversible amyloid toxin

Biochemistry

Volumn 44, Issue 29, 2005, Pages 9825-9832

  Fukui, Takashi ^a   Shiraki, Kentaro ^b   Hamada, Daizo ^a   Hara, Kojiro ^d   Miyata, Tomoko ^e   Fujiwara, Shinsuke ^c,g   Mayanagi, Kouta ^e   Yanagihara, Keiko ^a   Iida, Tetsuya ^d   Fukusaki, Eiichiro ^c   Imanaka, Tadayuki ^f   Honda, Takeshi ^d   Yanagihara, Itaru ^a  

^a RESEARCH INSTITUTE FOR MATERNAL AND CHILD HEALTH   (Japan)

^b UNIVERSITY OF TSUKUBA   (Japan)

^c OSAKA UNIVERSITY   (Japan)

^d OSAKA UNIVERSITY   (Japan)

^e BIOMOL ENG RESEARCH INSTITUTE   (Japan)

^f KYOTO UNIVERSITY   (Japan)

^g KWANSEI GAKUIN UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

COOLING; DETOXIFICATION; HEATING; TOXICITY; TRANSMISSION ELECTRON MICROSCOPY;

ARRHENIUS EFFECTS; SLOW COOLING; THERMOSTABLE DIRECT; VIBRIO PARAHAEMOLYTICUS;

BACTERIA;

AMYLOID; CONGO RED; GANGLIOSIDE GT 1B; HEMOLYSIN; THERMOSTABLE DIRECT HEMOLYSIN; THIOFLAVINE; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

ARTICLE; BETA SHEET; COOLING; DETOXIFICATION; DISSOCIATION; DOSE RESPONSE; FLUORESCENCE; HEATING; HEMOLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; THERMOSTABILITY; TRANSMISSION ELECTRON MICROSCOPY; VIBRIO PARAHAEMOLYTICUS;

AMYLOID; AMYLOID BETA-PROTEIN; ANIMALS; BACTERIAL PROTEINS; BACTERIAL TOXINS; CIRCULAR DICHROISM; CONGO RED; HEAT; HEMOLYSIN PROTEINS; MODELS, BIOLOGICAL; MODELS, CHEMICAL; MOLECULAR WEIGHT; PROTEIN CONFORMATION; RABBITS; SPECTROMETRY, FLUORESCENCE; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; THIAZOLES; VIRULENCE FACTORS;

ARRHENIUS; VIBRIO PARAHAEMOLYTICUS;

EID: 22744437693     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050311s     Document Type: Article

References (45)

1. Miwatani, T., Takeda, Y., Sakurai, J., Yoshihara, A., and Taga, S. (1972) Effect of heat (Arrhenius effect) on crude hemolysin of Vibrio parahaemolyticus, Infect. Immun. 6, 1031-1033.
2. Arrhenius, S. (1907) Anwendungen der physikalischen Chemie auf die Lehre von den physiologischen Antikoerpern, Immunochemie, Akademische Verlagsgesellschaft, Leipzig, Germany.
3. Vasil, M. L., Liu, P. V., and Iglewski, B. H. (1976) Temperature- dependent inactivation factor of Pseudomonas aeruginosa exotoxin A, Infect. Immun. 13, 1467-1472.
4. Coolbaugh, J. C., and Williams, R. P. (1978) Production and characterization of two hemolysins of Bacillus cereus, Can. J. Microbiol. 24, 1289-1295.
5. Albesa, I., Barberis, L. I., Pajaro, M. C., Farnochi, M. C., and Eraso, A. J. (1985) A thiol-activated hemolysin in gram-negative bacteria, Can. J. Microbiol. 31, 297-300.
6. Iida, T., and Honda, T. (1997) Hemolysins produced by Vibrios, J. Toxicol. Toxin Rev. 16, 215-227.
7. T1, Infect. Immun. 14, 1-5.
8. Honda, T., Ni, Y., and Miwatani, T. (1992) The thermostable direct hemolysin of Vibrio parahaemolyticus is a pore-forming toxin, Can. J. Microbiol. 38, 1175-1180.
9. Song, L., Hobaugh, M. R., Shustak, C., Cheley, S., Bayley, H., and Gouaux, J. E. (1996) Structure of staphylococcal α-hemolysin, a heptameric transmembrane pore, Science 274, 1859-1866.
10. Palmer, M., Harris, R., Freytag, C., Kehoe, M., Tranum-Jensen, J., and Bhakdi, S. (1998) Assembly mechanism of the oligomeric streptolysin O pore: The early membrane lesion is lined by a free edge of the lipid membrane and is extended gradually during oligomerization, EMBO J. 17, 1598-1605.
11. Gilbert, R. J. C., Jiménez, J. L., Chen, S., Tickle, I. J., Rossjohn, J., Parker, M., Andrew, P. W., and Saibil, H. R. (1999) Two structural transitions in membrane pore formation by pneumolysin, the pore-forming toxin of Streptococcus pneumoniae, Cell 97, 647-655.
12. Wallace, A. J., Stillman, T. J., Atkins, A., Jamieson, S. J., Bullough, P. A., Green, J., and Artymiuk, P. J. (2000) E. coli hemolysin E (HlyE, ClyA, SheA): X-ray crystal structure of the toxin and observation of membrane pores by electron microscopy, Cell 100, 265-276.
13. Naim, R., Yanagihara, I., Iida, T., and Honda, T. (2001) Vibrio parahaemolyticus thermostable direct hemolysin can induce an apoptotic cell death in Rat-1 cells from inside and outside of the cells, FEMS Microbiol. Lett. 195, 237-244.
14. Carrell, R. W., and Gooptu, B. (1998) Conformational changes and disease: Serpins, prions and Alzheimer's, Curr. Opin. Struct. Biol. 8, 799-809.
15. Chiti, F., Webster, P., Taddei, N., Clark, A., Stefani, M., Ramponi, G., and Dobson, C. M. (1999) Designing conditions for in vitro formation of amyloid protofilaments and fibrils, Proc. Natl. Acad. Sci. U.S.A. 96, 3590-3594.
16. Chiti, F., Taddei, N., Bucciantini, M., White, P., Ramponi, G., and Dobson, C. M. (2000) Mutational analysis of the propensity for amyloid formation by a globular protein, EMBO J. 19, 1441-1449.
17. Chiti, F., Bucciantini, M., Capanni, C., Taddei, N., Dobson, C. M., and Stefani, M. (2001) Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain, Protein Sci. 10, 2541-2547.
18. Fändrich, M., Fletcher, M. A., and Dobson, C. M. (2001) Amyloid fibrils from muscle myoglobin, Nature 410, 165-166.
19. Guijarro, J. I., Sunde, M., Jones, J. A., Campbell, D., and Dobson, C. M. (1998) Amyloid fibril formation by an SH3 domain, Proc. Natl. Acad. Sci. U.S.A. 95, 4224-4228.
20. Hamada, D., and Dobson, C. M. (2002) A kinetic study of β-lactoglobulin amyloid fibril formation promoted by urea, Protein Sci. 11, 2411-2426.
21. Chiti, F., Stefani, M., Taddei, N., Ramponi, G., and Dobson, C. M. (2003) Rationalization of the effects of mutations on peptide and protein aggregation rates, Nature 424, 805-808.
22. DuBay, K. F., Pawar, A. P., Chiti, F., Zurdo, J., Dobson, C. M., and Vendruscolo, M. (2004) Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains, J. Mol. Biol. 341, 1317-1326.
23. Kelly, J. W. (1996) Alternative conformations of amyloidogenic proteins govern their behavior, Curr. Opin. Struct. Biol. 6, 11-17.
24. Prusiner, S. B., Scott, M. R., DeArmond, S. J., and Cohen, F. E. (1998) Prion protein biology, Cell 93, 337-348.
25. Jiménez, J. L., Guijarro, J. I., Orlova, E., Zurdo, J., Dobson, C. M., Sunde, M., and Saibil, R. (1999) Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing, EMBO J. 18, 815-821.
26. Cohen, F. E., Pan, K. M., Huang, Z., Baldwin, M., Fletterick, R. J., and Prusiner, S. B. (1994) Structural clues to prion replication, Science 264, 530-531.
27. Jarrett, J. T., and Lansbury, P. T., Jr. (1993) Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73, 1055-1058.
28. Tang, G. Q., Iida, T., Yamamoto, K., and Honda, T. (1994) A mutant toxin of Vibrio parahaemolyticus thermostable direct hemolysin which has lost hemolytic activity but retains ability to bind to erythrocytes, Infect. Immun. 62, 3299-3304.
29. McLaurin, J., and Chakrabartly, A. (1996) Membrane disruption by Alzheimer β-amyloid peptides mediated through specific binding to either phospholipids or gangliosides, J. Biol. Chem. 271, 26482-26489.
30. Yanagihara, I., Inui, K., Dickson, G., Turner, G., Piper, T., Kaneda, Y., and Okada, S. (1996) Expression of full-length human dystrophin cDNA in mdx mouse muscle by HVJ-liposome injection, Gene Ther. 3, 549-553.
31. Naiki, H., Higuchi, K., Hosokawa, M., and Takeda, T. (1989) Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavin T, Anal. Biochem. 177, 244-249.
32. Li, S. C., and Deber, C. M. (1994) A measure of helical propensity for amino acids in membrane environments, Nat. Struct. Biol. 1, 368-373.
33. Kagan, B. L., Hirakura, Y., Azimov, R., Azimova, R., and Lin, M. C. (2002) The channel hypothesis of Alzheimer's disease: Current status, Peptides 23, 1311-1315.
34. Kourie, J. I., and Henry, C. L. (2002) Ion channel formation and membrane-linked pathologies of misfolded hydrophobic proteins: The role of dangerous unchaperoned molecules, Clin. Exp. Pharmacol Physiol. 29, 741-753.
35. Mattson, M. P., Begley, J. G., Mark, R. J., and Furukawa, K. (1997) Aβ25-35 induces rapid lysis of red blood cells: Contrast with Aβ1-42 and examination of underlying mechanisms, Brain Res. 771, 147-153.
36. 2-Microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro, J. Mol. Biol. 313, 559-571.
37. 2-microglobulin studied by heteronuclear NMR, Protein Sci. 11, 2218-2229.
38. Tan, S. Y., and Pepys, M. B. (1994) Amyloidosis, Histopathology 25, 403-414.
39. Kelly, J. W. (2002) Towards an understanding of amyloidogenesis, Nat. Struct. Biol. 9, 323-325.
40. Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., and Stefani, M. (2002) Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases, Nature 416, 507-511.
41. Shatursky, O., Heuck, A. P., Shepard, L. A., Rossjohn, J., Parker, M. W., Johnson, A. E., and Tweten, R. K. (1999) The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for pore-forming toxins, Cell 99, 293-299.
42. Ramachandran, R., Tweten, R. K., and Johnson, A. E. (2004) Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit β-strand aliment, Nat. Struct. Mol. Biol. 11, 697-705.
43. Lang, P. A., Kaiser, S., Myssina, S., Birka, C., Weinstock, C., Northoff, H., Wieder, T., Lang, F., and Huber, S. M. (2004) Effect of Vibrio parahaemolyticus haemolysin on human erythrocytes, Cell. Microbiol. 6, 391-400.
44. MI, ganglioside-bound amyloid β-protein (Aβ): A possible form of preamyloid in Alzheimer's disease, Nat. Med. 1, 1062-1066.
45. Choo-Smith, L. P., Garzon-Rodriguez, W., Glabe, C. G., and Surewicz, W. K. (1997) Acceleration of amyloid fibril formation by specific binding of Aβ-(1-40) peptide to ganglioside-containing membrane vesicles, J. Biol. Chem. 272, 22987-22990.