Advanced search
Publication Cover
Bioscience, Biotechnology, and Biochemistry Volume 65, 2001 - Issue 12
Journal homepage
169
Views
8
CrossRef citations to date
0
Altmetric
Original Articles

Mutational and Comparative Analysis of Streptolysin O, an Oxygen-labile Streptococcal Hemolysin

Ikkyu YAMAMOTODepartment of Biochemistry I, Fukui Medical University
,
Hisashi KIMOTODepartment of Biochemistry I, Fukui Medical University
,
Yoriko TAKETODepartment of Pharmacology, Kanazawa University School of Medicine
&
Akira TAKETODepartment of Biochemistry I, Fukui Medical University;Department of Applied Physics and Chemistry, Fukui University of Technology
Pages 2682-2689 | Received 19 Jun 2001, Accepted 30 Aug 2001, Published online: 22 May 2014

  • 1) Halbert, P., Streptolysin O. In “Microbial toxins”, eds. Montie, T.C., Kadis, A.S., and Ajl, S.J., Academic Press, New York, pp. 69-98 (1970).
  • 2) Alouf, J.E., Streptococcal toxin (streptolysin O, streptolysin S, erythrogenic toxin). Pharmac. Ther., 11, 661-717 (1980).
  • 3) Alouf, J.E. and Geoffroy, C., The family of the antigenically related, cholesterol-binding (‘sulfhydryl-activated’) cytolytic toxins. In “Sourcebook of bacterial protein toxins” eds. Alouf, J.E. and Freer, J.H., Academic Press, London, pp. 147-186 (1991).
  • 4) Bhakdi, S., Weller, U., Walev, I., Martin, E., Jonas, D., and Palmer, M.A guide to the use of poreforming toxins for controlled permeabilization of cell membranes. Med. Microbiol. Immunol., 182, 167-175 (1993).
  • 5) Pinkney, M., Kapur, V., Smith, J., Weller, U., Palmer, M., Glanville, M., Messner, M., Musser, J.M., Bhakdi, S., and Kehoe, M.A., Different forms of streptolysin O produced by Steptococcus pyogenes and by Escherichia coli expressing recombinant toxin: cleavage by streptococcal cysteine protease. Infect. Immun., 63, 2776-2779 (1995).
  • 6) Weller, U., Muller, L., Messner, M., Palmer, M., Valeva, A., Tranum-Jensen, J., Agrawal, P., Biermann, C., Dobereiner, A., Kehoe M.A., and Bhakdi, S., Expression of active streptolysin O in Escherichia coli as a maltose-binding-protein-streptolysin O fusion protein The N-terminal 70 amino acids are not required for hemolytic activity. Eur. J. Biochem., 236, 34-39 (1996).
  • 7) Palmer, P., Saweljew, P., Vulicevic, I., Valeva, A., Kehoe, M., and Bhakdi, S., Membrane-penetrating domain of streptolysin O identified by cysteine scanning mutagenesis. J. Biol. Chem., 271, 26664-26667 (1996).
  • 8) Taketo, A. and Taketo, Y., Biochemical studies on streptolysin S formation I. Streptolysin S formation in cell free system. J. Biochem., 56, 552-561 (1964).
  • 9) Kimoto, H. and Taketo, A., Initial stage of DNA-electrotransfer into E. coli cells. J. Biochem., 122, 237-242 (1997).
  • 10) Taketo, A. and Taketo, Y., Cytolytic effect of streptolysin S complex on Ehrlich ascites tumor cells. J. Biochem., 60, 357-362 (1966).
  • 11) Kehoe, M.A., Miller, L., Walker, J.A., and Boulnois, G.J., Nucleotide sequence of the streptolysin O (SLO) gene: Streuctural homologies between SLO and other membrane-damaging, thiol-activated toxins. Infect. Immun., 55, 3228-3232 (1987).
  • 12) Chou, P.Y. and Fasman, G.D., Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzymol. Relat. Areas Mol. Biol., 47, 45-148 (1978).
  • 13) Garnier, J., Osguthorpe, D.J., and Robson, B., Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J. Mol. Biol., 25, 97-120 (1978).
  • 14) Taketo, A. and Taketo, Y., Biochemical studies on streptolysin S formation III. Intracellular streptolysins. J. Biochem., 57, 787-792 (1965).
  • 15) Calandra, G.B. and Theodore, T.S., Cellular location of streptolysin O. Infect. Immun., 12, 750-753 (1975).
  • 16) Rossjohn, J., Feil, S.C., McKinstrey, W.J., Tweten, R.K., and Parker, M.W., Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. Cell, 89, 685-692 (1997).
  • 17) Bayley, H., Toxin structure: Part of a hole?. Current Biol., 7, R763-R767 (1997).
  • 18) Ghani, E.M.A., Weis, S., Walev, I., Kehoe, M., Bhakdi, S., and Palmer, M., Streptolysin O: Inhibition of the conformational change during membrane binding of the monomer prevents oligomerization and pore formation. Biochemistry, 38, 15204-15211 (1999).
  • 19) Shatursky, O., Heuck, A.P., Shepard, L.A., Rossjohn, J., Parker, M.W., Johnson A.E., and Tweten, R.K., The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins. Cell, 99, 293-299 (1999).
  • 20) Bhakdi, S., Bayley, H., Valeva, A., Walev, I., Walker, B., Weller, U., Kehoe, M., and Palmer, M., Staphylococcal alpha-toxin, streptolysin O, and Escherichia coli hemolysin: prototypes of pore-forming bacterial cytolysins. Arch. Mikrobiol., 165, 73-79 (1996).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.