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REFERENCES

  • 1
    Stevens D.L., Musher D.M., Watson D.A., Eddy H., Hamill R.J., Gyorkey F., Rosen H., Mader J. (1990) Spontaneous, nontraumatic gangrene due to Clostridium septicum. Rev of Infect Dis 12: 28696.
  • 2
    Wilson L.M., Macfarlane G.T. (1996) Cytotoxicity, adhesion and invasion of Clostridium septicum in cultured human epithelial cells (CACO-2, HEp-2): pathological significance of swarm cell differentiation. Anaerobe 2: 719.
  • 3
    Smith D.D.L. (1975) Clostridium septicum. In: Charles C.T., eds. The Pathogenic Anaerobic Bacteria, 3rd edn. Illinois: Springfield, pp. 24555.
  • 4
    Ballard J., Bryant A., Stevens D., Tweten R.K. (1992) Purification and characterization of the lethal toxin (alpha-toxin) of Clostridium septicum. Infect Immun 60: 78490.
  • 5
    Gordon V.M., Benz R., Fujii K., Leppla S.H., Tweten R.K. (1997) Clostridium septicum alpha-toxin is proteolytically activated by furin. Infect Immun 65: 41304.
  • 6
    Ballard J., Crabtree J., Roe B.A., Tweten R.K. (1995) The primary structure of Clostridium septicum alpha-toxin exhibits similarity with that of Aeromonas hydrophila aerolysin. Infect Immun 63: 3404.
  • 7
    Cole A.R., Gilbert M., Popoff M., Moss D.S., Titball R.W., Basak A.K. (2004) Clostridium perfringens epsilon-toxin shows structural similarity to the pore-forming toxin aerolysin. Nat Struct Mol Biol 11: 7978.
  • 8
    Ballard J., Sokolov Y., Yuan W.L., Kagan B.L., Tweten R.K. (1993) Activation and mechanism of Clostridium septicum alpha toxin. Mol Microbiol 10: 62734.
  • 9
    Imagawa T., Dohi Y., Higashi Y. (1994) Cloning, nucleotide sequence and expression of a hemolysin gene of Clostridium septicum. FEMS Microbiol Lett 117: 28792.
  • 10
    Gordon V.M., Nelson K.L., Buckley J.T., Stevens V.L., Tweten R.K., Elwood P.C., Leppla S.H. (1999) Clostridium septicum alpha toxin uses glycosylphosphatidylinositol-anchored protein receptors. J Biol Chem 274: 2727480.
  • 11
    Wichroski M.J., Melton J.A., Donahue C.G., Tweten R.K., Ward G.E. (2002) Clostridium septicum alpha-toxin is active against the parasitic protozoan Toxoplasma gondii and targets members of the SAG family of glycosylphosphatidylinositol-anchored surface proteins. Infect Immun 70: 435361.
  • 12
    Hang'ombe M.B., Mukamoto M., Kohda T., Sugimoto N., Kozaki S. (2004) Cytotoxicity of Clostridium septicum alpha-toxin: its oligomerization in detergent resistant membranes of mammalian cells. Microbiol Pathog 37: 27986.
  • 13
    Sellman B.R., Tweten R.K. (1997) The propeptide of Clostridium septicum alpha toxin functions as an intramolecular chaperone and is a potent inhibitor of alpha toxin-dependent cytolysis. Mol Microbiol 25: 42940.
  • 14
    Melton J.A., Parker M.W., Rossjohn J., Buckley J.T., Tweten R.K. (2004) The identification and structure of the membrane-spanning domain of the Clostridium septicum alpha toxin. J Biol Chem 279: 14,31522.
  • 15
    Parker M.W., van der Goot F.G., Buckley J.T. (1996) Aerolysin – the ins and outs of a model channel-forming toxin. Mol Microbiol 19: 20512.
  • 16
    Melton-Witt J.A., Bentsen L.M., Tweten R.K. (2006) Identification of functional domains of Clostridium septicum alpha toxin. Biochemistry 45: 14,34754.
  • 17
    Tweten R.K. (1988) Nucleotide sequence of the gene for perfrigolysin O (theta toxin) from Clostridium perfringens: significant homology with the genes for streptolysin and pneumolysin. Infect Immun 56: 323540.
  • 18
    Kehoe M.A., Miller L., Walker J.A., Boulnois G.J. (1987) Nucleotide sequence of the streptolysin O (SLO) gene: structural homologies between SLO and other membrane, thiol-activated toxins. Infect Immun 55: 322832.
  • 19
    Walker J.A., Allen R.L., Falmagne P., Johnson M.K., Boulnois G.J. (1987) Molecular cloning, characterization and complete nucleotide sequence of the gene for pneumolysin, the sulfhydryl-activated toxin of Streptococcus pneumoniae. Infect Immun 55: 11849.
  • 20
    Mengaud J., Chenevert J., Geoffroy C., Gaillard J., Cossart P. (1987) Identification of the structural gene encoding the SH-activated hemolysin of Listeria monocytogenes: listeriolysin O is homologous to streptolysin O and pneumolysin. Infect Immun 55: 32257.
  • 21
    Sekino-Suzuki N., Nakamura M., Mitsui K., Ohno-Iwashita Y. (1996) Contribution of individual tryptophan residues to the structure and activity of theta-toxin (perfringolysin O), a cholesterol-binding cytolysin. Eur J Biochem 241: 9417.
  • 22
    Laemmli U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 6805.
  • 23
    Miyata S., NMatsushita O., Minami J., Katayama S., Shimamoto S., Okabe A., (2001) Cleavage of a C-terminal peptide is essential for heptamerization of Clostridium perfringens epsilon-toxin in the synaptosomal membrane. J Biol Chem 276: 13,77883.
  • 24
    Nelson K.L., Raja S.M., Buckley J.T. (1997) The glycosylphosphatidylinositol-anchored surface glycoprotein Thy-1 is a receptor for the channel-forming toxin. J Biol Chem 272: 12,17074.
  • 25
    Hang'ombe M.B., Kohda T., Mukamoto M., Kozaki S. (2005) Relationship between Clostridium septicum alpha-toxin activity and binding to erythrocyte membranes. J Vet Med Sci 67: 6974.
  • 26
    Bradford M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bunding. Anal Biochem 72: 24854.
  • 27
    Hong, Y., Ohishi, K., Inoue, N., Kang, J.Y., Shime, H., Horiguchi, Y., van der Goot, F.G., Sugimoto, N., Kinoshita, T. (2002) Requirement of N-glycan on GPI-anchored proteins for efficient binding of aerolysin but not Clostridium septicum α-toxin. EMBO J 21: 504756.