Relationship between heat-induced fibrillogenicity and hemolytic activity of thermostable direct hemolysin and a related hemolysin of Vibrio parahaemolyticus

FEMS Microbiology Letters

Volumn 318, Issue 1, 2011, Pages 10-17

  Ohnishi, Kiyouhisa ^a   Nakahira, Kumiko ^a   Unzai, Satoru ^b   Mayanagi, Kouta ^c   Hashimoto, Hiroshi ^b   Shiraki, Kentaro ^d   Honda, Takeshi ^e   Yanagihara, Itaru ^a  

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

^b YOKOHAMA CITY UNIVERSITY   (Japan)

^c KYUSHU UNIVERSITY   (Japan)

^d UNIVERSITY OF TSUKUBA   (Japan)

^e OSAKA UNIVERSITY   (Japan)

Author keywords

Arrhenius effect; Fibrillogenicity; Tetrameric structure; Thermostable direct hemolysin related hemolysin

Indexed keywords

AMYLOID PROTEIN; HEMOLYSIN; THERMOSTABLE DIRECT HEMOLYSIN; THERMOSTABLE DIRECT HEMOLYSIN RELATED HEMOLYSIN; THIOFLAVINE; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

AMINO ACID SEQUENCE; BACTERIAL VIRULENCE; CIRCULAR DICHROISM; CONTROLLED STUDY; ERYTHROCYTE MEMBRANE; GEL PERMEATION CHROMATOGRAPHY; HEAT; HEATING; HEMOLYSIS; HUMAN; HUMAN CELL; LETTER; MEMBRANE DAMAGE; MOLECULAR MODEL; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; THERMOSTABILITY; TRANSMISSION ELECTRON MICROSCOPY; ULTRACENTRIFUGATION; ULTRAVIOLET SPECTROSCOPY; VIBRIO PARAHAEMOLYTICUS;

BACTERIAL TOXINS; CIRCULAR DICHROISM; ERYTHROCYTES; HEMOLYSIN PROTEINS; HEMOLYSIS; HOT TEMPERATURE; HUMANS; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; VIBRIO PARAHAEMOLYTICUS; VIRULENCE FACTORS;

VIBRIO PARAHAEMOLYTICUS;

EID: 79953327301     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2011.02233.x     Document Type: Letter

References (31)

1. Arrhenius S (1907) Immunochemie. Anwendungen der physikalischen Chemie auf die Lehre von den physiologichen Antikoerpern. Akademische Verlagsgesellschaft, Leipzig.
2. Blake PA, Weaver RE & Hollis DG (1980) Diseases of humans (other than cholera) caused by vibrios. Annu Rev Microbiol 34: 341-367.
3. Bucciantini M, Giannoni E, Chiti F, Baroni F, Formibli L, Zurdo J, Taddei N, Ramponi G, Dobson CM & Stefani M (2002) Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416: 507-511.
4. Daniels NA, Mackinnon L, Bishop R et al. (2000) Vibrio parahaemolyticus infections in the United States, 1973-1998. J Infect Dis 181: 1661-1666.
5. Fukui T, Shiraki K, Hamada D et al. (2005) Thermostable direct hemolysin of Vibrio parahaemolyticus is a bacterial reversible amyloid toxin. Biochemistry 44: 9825-9832.
6. Haataja L, Gurlo T, Huang CJ & Butler PC (2008) Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis. Endocr Rev 29: 303-316.
7. Hamada D & Dobson CM (2002) A kinetic study of β-lactoglobulin amyloid fibril formation promoted by urea. Protein Sci 11: 2411-2426.
8. Hamada D, Higurashi T, Mayanagi K, Miyata T, Fukui T, Iida T, Honda T & Yanagihara I (2007) Tetrameric structure of thermostable direct hemolysin from Vibrio parahaemolyticus revealed by ultracentrifugation, small-angle X-ray scattering and electron microscopy. J Mol Biol 365: 187-195.
9. Hardy J & Selkoe DJ (2002) The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297: 353-356.
10. Hardy PS, Nakano M & Iida T (2004) Single channel evidence for innate pore-formation by Vibrio parahaemolyticus thermostable direct haemolysin (TDH) in phospholipid bilayers. FEMS Microbiol Lett 240: 81-85.
11. Honda T & Iida T (1993) The pathogenicity of Vibrio parahaemolyticus and the role of the thermostable direct hemolysin and related hemolysin. Rev Med Microbiol 4: 106-113.
12. Honda T, Chearskul S, Takeda Y & Miwatani T (1980) Immunological methods for detection of Kanagawa negative Vibrio parahaemolyticus. Lancet i: 331-332.
13. Honda T, Ni Y & Miwatani T (1988) Purification and characterization of a hemolysin produced by a clinical isolated of Kanagawa phenomenon-negative Vibrio parahaemolyticus and related to the thermostable direct hemolysin. Infect Immun 56: 961-965.
14. Honda T, Ni Y & Miwatani T (1992) The thermostable direct hemolysin of Vibrio parahaemolyticus is a pore-forming toxin. Can J Microbiol 38: 1175-1180.
15. Iida T & Honda T (1997) Hemolysins produced by Vibrios. J Toxicol-Toxin Rev 16: 215-227.
16. Jang H, Arce FT, Ramachandran S, Capone R, Azimova R, Kagan BL, Nussinov R & Lal R (2010) Truncated beta-amyloid peptide channels provide an alternative mechanism for Alzheimer's disease and Down syndrome. P Natl Acad Sci USA 107: 6538-6543.
17. Joseph SW, Colwell RR & Kaper JB (1982) Vibrio parahaemolyticus and related halophilic vibrios. Crit Rev Microbiol 10: 77-124.
18. Kishishita M, Matsuoka N, Kumagai K, Yamasaki S, Takeda Y & Nishibuchi M (1992) Sequence variation in the thermostable direct hemolysin-related hemolysin (trh) gene of Vibrio parahaemolyticus. Appl Environ Microb 58: 2449-2457.
19. Lesné S, Koh MT, Kotilinek L, Kayed R, Glabe CG, Yang A, Gallagher M & Ashe KH (2006) A specific amyloid-beta protein assembly in the brain impairs memory. Nature 440: 352-357.
20. Marti-Renom MA, Stuart AC, Fiser A, Sanchez R, Melo F & Sali A (2000) Comparative protein structure modeling of genes and genomes. Annu Rev Bioph Biom 29: 291-325.
21. Miwatani T, Takeda Y, Sakurai J, Yoshihara A & Taga S (1972) Effect of heat (Arrhenius effect) on crude hemolysin of Vibrio parahaemolyticus. Infect Immun 6: 1031-1033.
22. Naim R, Yanagihara I, Iida T & 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.
23. Nishibuchi M, Taniguchi T, Misawa T, Khaeomanee-Iam V, Honda T & Miwatani T (1989) Cloning and nucleotide sequence of the gene (trh) encoding the hemolysin related to the thermostable direct hemolysin of Vibrio parahaemolyticus. Infect Immun 57: 2691-2697.
24. Okuda J & Nishibuchi M (1998) Manifestation of the Kanagawa phenomenon, the virulence-associated phenotype, of Vibrio parahaemolyticus depends on a particular single base change in the promoter of the thermostable direct haemolysin gene. Mol Microbiol 30: 499-511.
25. Quist A, Doudevski I, Lin H, Azimova R, Ng D, Frangione B, Kagan B, Ghiso J & Lal R (2005) Amyloid ion channels: a common structural link for protein-misfolding disease. P Natl Acad Sci USA 102: 10427-10432.
26. Raimondi F, Kao JPY, Fiorentini C, Fabbri A, Donelli G & Gasparini N (2000) Enterotoxicity and cytotoxicity of Vibrio parahaemolyticus thermostable direct hemolysin in vitro systems. Infect Immun 68: 3180-3185.
27. Shibayama N (2008) Circular dichroism study on the early folding events of β-lactoglobulin entrapped in wet silica gels. FEBS Lett 582: 2668-2672.
28. Shirai H, Ito H, Hirayama T, Nakamoto Y, Nakabayashi N, Kumagai K, Takeda Y & Nishibuchi M (1990) Molecular epidemiologic evidence for association of thermostable direct hemolysin (TDH) and TDH-related hemolysin of Vibrio parahaemolyticus with gastroenteritis. Infect Immun 58: 3568-3573.
29. Sreerama N & Woody RW (2000) Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal Biochem 287: 252-260.
30. Uversky VN & Fink AL (2004) Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim Biophys Acta 1698: 131-153.
31. Yanagihara I, Nakahira K, Yamane T et al. (2010) Structure and functional characterization of Vibrio parahaemolyticus thermostable direct hemolysin. J Biol Chem 285: 16267-16274.