Site-directed mutagenesis of Clostridium perfringens beta-toxin: Expression of wild-type and mutant toxins in Bacillus subtilis

FEMS Microbiology Letters

Volumn 158, Issue 1, 1998, Pages 17-23

  Steinthorsdottir, Valgerdur ^a   Fridriksdottir, Vala ^a   Gunnarsson, Eggert ^a   Andrésson, Ólafur S ^a  

^a UNIVERSITY OF ICELAND   (Iceland)

Author keywords

Beta toxin; Biological activity; Clostridium perfringens; Mutagenesis

Indexed keywords

CLOSTRIDIUM TOXIN; MUTANT PROTEIN; STAPHYLOCOCCUS TOXIN;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; BACILLUS SUBTILIS; CLOSTRIDIUM PERFRINGENS; FEMALE; LETHAL DOSE; MALE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; RABBIT; SHEEP; SITE DIRECTED MUTAGENESIS; TOXIN ANALYSIS;

ANIMALIA; BACILLUS SUBTILIS; BACTERIA (MICROORGANISMS); CLOSTRIDIUM; CLOSTRIDIUM PERFRINGENS; ORYCTOLAGUS CUNICULUS; OVIS ARIES; POSIBACTERIA; STAPHYLOCOCCUS; STAPHYLOCOCCUS AUREUS;

EID: 0031887515     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(97)00470-9     Document Type: Article

References (23)

1. Sakurai, J. and Duncan, C.L. (1977) Purification of beta-toxin from Clostridium perfringens type C. Infect. Immun. 18, 741-745.
2. Sakurai, J. and Duncan, C.L. (1978) Some properties of beta-toxin produced by Clostridium perfringens type C. Infect. Immun. 21, 678-680.
3. Sakurai, J. and Fujii, Y. (1987) Purification and characterization of Clostridium perfringens beta toxin. Toxicon 25, 1301-1310.
4. Sakurai, J., Fujii, Y., Matsuura, M. and Endo, K. (1981) Pharmacological effect of beta toxin of Clostridium perfringens type C on rats. Microbiol. Immunol. 25, 423-432.
5. Steinthorsdottir, V., Fridriksdottir, V., Gunnarsson, E. and Andrésson, Ó.S. (1995) Expression and purification of Clostridium perfringens beta-toxin glutathione S-transferase fusion protein. FEMS Microbiol. Lett. 130, 273-278.
6. Hunter, S.E.C., Brown, J.E., Oyston, P.C.F., Sakurai, J. and Titball, R.W. (1993) Molecular genetic analysis of the beta-toxin of Clostridium perfringens reveals sequence homology with the alpha-toxin, gamma-toxin and leukocidin of Staphylococcus aureus. Infect. Immun. 61, 3958-3965.
7. Prévost, G., Cribier, B., Couppié, P., Petiau, P., Supersac, G., Finck-Barbançon, V., Monteil, H. and Piemont, Y. (1995) Panton-Valentine leucocidin and gamma-hemolysin from Staphylococcus aureus ATCC 49775 are encoded by distinct genetic loci and have different biological activities. Infect. Immun. 63, 4121-4129.
8. Bhakdi, S. and Tranum-Jensen, J. (1991) Alpha-toxin of Staphylococcus aureus. Microbiol. Rev. 55, 733-751.
9. Gouaux, J.E., Braha, O., Hobaugh, M.R., Song, L., Cheley, S., Shustak, C. and Bayley, H. (1994) Subunit stoichiometry of staphylococcal α-hemolysin in crystals and on membranes: A heptameric transmembrane pore. Proc. Natl. Acad. Sci. USA 91, 12828-12831.
10. 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.
11. Jursch, R., Hildebrand, A., Hobom, G., Tranum-Jensen, J., Ward, R., Kehoe, M. and Bhakdi, S. (1994) Histidine residues near the N terminus of staphylococcal alpha-toxin as reporters of regions that are critical for oligomerization and pore formation. Infect. Immun. 62, 2249-2256.
12. Menzies, B.E. and Kernodle, D.S. (1994) Site-directed mutagenesis of the alpha-toxin gene of Staphylococcus aureus: Role of histidines in toxin activity in vitro and in a murine model. Infect. Immun. 62, 1843-1847.
13. Walker, B. and Bayley, H. (1995) Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal α-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification. J. Biol. Chem. 270, 23065-23071.
14. Sakurai, J., Fujii, Y. and Matsuura, M. (1980) Effect of oxidizing agents and sulfhydryl group reagents on beta toxin from Clostridium perfringens type C. Microbiol. Immunol. 24, 595-601.
15. Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A. and Struhl, K. (1987) Current Protocols in Molecular Biology. Wiley Interscience, New York.
16. Gryczan, T.J., Contente, S. and Dubnau, D. (1978) Characterization of Staphylococcus aureus plasmids introduced by transformation into Bacillus subtilis. J. Bacteriol. 134, 318-329.
17. Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
18. Hansen, K.M., Frandsen, P.L. and Meyling, A. (1992) Monoclonal antibodies against Clostridium perfringens type C beta-toxin. Production and characterization. In: Bacterial Protein Toxins: Fifth Workshop, Veldhofen, June 30-July 5, 1991 (Witholt, B. et al., Eds.), pp. 75-76. Gustav Fischer, New York.
19. Spouge, J.L. (1992) Statistical analysis of sparse infection data and its implications for retroviral treatment trials in primates. Proc. Natl. Acad. Sci. USA 89, 7581-7585.
20. Simonen, M. and Palva, I. (1993) Protein secretion in Bacillus species. Microbiol. Rev. 57, 109-137.
21. Ward, R.J., Palmer, M., Leonard, K. and Bhakdi, S. (1994) Identification of a putative membrane-inserted segment in the alpha-toxin of Staphylococcus aureus. Biochemistry 33, 7477-7484.
22. Hildebrand, A., Pohl, M. and Bhakdi, S. (1991) Staphylococcus aureus alpha-toxin: dual mechanism of binding to target cells. J. Biol. Chem. 266, 17195-17200.
23. Bhakdi, S., Grimminger, F., Suttorp, N., Walmrath, D. and Seeger, W. (1994) Proteinaceous bacterial toxins and pathogenesis of sepsis syndrome and septic shock: the unknown connection. Med. Microbiol. Immunol. 183, 119-144.