Immunological and functional comparison between Clostridium perfringens iota toxin, C. spiroforme toxin, and anthrax toxins

FEMS Microbiology Letters

Volumn 146, Issue 1, 1997, Pages 117-121

  Perelle, Sylvie ^a   Scalzo, Salvatore ^a   Kochi, Sims ^a   Mock, Michèle ^a   Popoff, Michel R ^a  

^a INSTITUT PASTEUR   (France)

Author keywords

anthrax toxin; Bacillus anthracis; Clostridium perfringens iota toxin; Clostridium spiroforme toxin

Indexed keywords

ANTHRAX TOXIN; CLOSTRIDIUM TOXIN;

ANTHRAX; ARTICLE; CELL MEMBRANE; CLOSTRIDIUM PERFRINGENS; CONTROLLED STUDY; ENZYME LINKED IMMUNOSORBENT ASSAY; IMMUNOLOGY; NONHUMAN; PRIORITY JOURNAL; TOXIN ANALYSIS;

EID: 0031016925     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(96)00463-6     Document Type: Article

References (14)

1. Considine, R.V. and Simpson, L.L. (1991) Cellular and molecular actions of binary toxins possessing ADP-ribosyltransferase activity. Toxicon 29, 913-936.
2. Perelle, S., Gilbert, M., Boquet, P. and Popoff, M.R. (1993) Characterization of Clostridium perfringens iota-toxin genes and expression in Escherichia coli. Infect. Immun. 61, 5147-5156.
3. Vandekerckhove, J., Schering, B., Bärmann, M. and Aktories, K. (1987) Clostridium perfringens iota toxin ADP-ribosylates skeletal muscle actin in Arg-177. FEBS Lett. 255, 48-52.
4. Leppla, S. (1995) Anthrax toxins. In: Bacterial Toxins and Virulence Factors in Disease, (Moss, J. et al., Eds.), pp. 543-572, Marcel Dekker, New York.
5. Klimpel, K.R., Molloy, S.S., Thomas, G. and Leppla, S.H. (1992) Anthrax toxin protective antigen is activated by a cell surface protease with the sequence specificity and catalytic properties of furin. Proc. Natl. Acad. Sci. USA 89, 10277-10281.
6. Mock, M. and Ullmann, A. (1993) Calmodulin-activated bacterial adenylate cyclases as virulence factors. Trends Microbiol. Sci. 1, 187-192.
7. Popoff, M.R., Milward, F.W., Bancillon, B. and Boquet, P. (1989) Purification of the Clostridium spiroforme binary toxin and activity of the toxin on Hep-2 cells. Infect. Immun. 57, 2462-2469.
8. Pezard, C., Duflot, E. and Mock, M. (1993) Construction of Bacillus anthracis mutant strains producing a single toxin component. J. Gen. Microbiol. 139, 2459-2463.
9. Friedlander, A.M. (1986) Macrophages are sensitive to anthrax lethal toxin through an acid-dependent process. J. Biol. Chem. 261, 7123-7126.
10. Hansen, M.B., Nielsen, S.E. and Berg, K. (1989) Re-examination and further development of a precise and rapid dye method for measuring cell growth/cell cycle. J. Immunol. Methods 119, 203-210.
11. 2-terminal region of the Bacillus anthracis edema factor. In: Bacterial Protein Toxins Zbl. Bakt. Suppl. (Freer, J. et al., Eds.) pp. 271-272.
12. Yoshida, T., Chen, C., Zhang, M. and Wu, H.C. (1991) Disruption of the Golgi apparatus by brefeldin A inhibits the cytotoxicity of ricin, modeccin, and Pseudomonas toxin. Exp. Cell Res. 192, 389-395.
13. VanderSpek, J., Cassidy, D., Genbauffe, F., Huynh, P.D. and Murphy, J.R. (1994) An intact transmembrane helix 9 is essential for the efficient delivery of the diphtheria toxin catalytic domain to the cytosol of target cells. J. Biol. Chem. 269, 21455-21459.
14. Milne, J.C., Furlong, D., Hanna, P.C., Wall, J.S. and Collier, J. (1994) Anthrax protective antigen forms oligomers during intoxication of mammalian cells. J. Biol. Chem. 269, 20607-20612.