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Originally published In Press as doi:10.1074/jbc.M107401200 on September 6, 2001

J. Biol. Chem., Vol. 276, Issue 45, 41790-41796, November 9, 2001
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Similarities between Complement-mediated and Streptolysin S-mediated Hemolysis*

Abbey CarrDagger , Darren D. SledjeskiDagger , Andreas Podbielski§, Michael D. P. BoyleDagger , and Bernd Kreikemeyer§

From the Dagger  Department of Microbiology & Immunology, Medical College of Ohio, Toledo, Ohio 43614-5806 and the § Department of Medical Microbiology & Hygiene, University Hospital Rostock, Schillingallee 70, D-18055 Rostock, Germany

The oxygen-stable hemolysin streptolysin S (SLS) of Streptococcus pyogenes is encoded in part by the pel/sagA gene product. Antibodies to a synthetic peptide from the C terminus of the Pel/SagA open reading frame inhibited hemolysis mediated by both culture supernatants from multiple M serotypes of S. pyogenes isolates or a commercially available SLS preparation. Analysis of the SLS-mediated hemolytic reaction demonstrated that it was temperature- and concentration-dependent. Like complement-mediated hemolysis it conforms to the prediction of a one-hit mechanism of hemolysis. A number of intermediates in the SLS-mediated hemolysis of sheep erythrocytes could be distinguished. SLS could bind to erythrocytes below 17 °C; however, lysis could only occur at temperatures >23 °C. Following binding of SLS and washing, a papain-sensitive intermediate could be distinguished prior to insertion of the SLS complex into the erythrocyte membrane, which resulted in formation of a transmembrane pore and led to irreversible osmotic lysis of the cell. These intermediates were similar to those described previously during complement-mediated hemolysis.


* This work was supported in part by Deutsche Forschungsgemeinschaft Grant PO 391/8-1 and National Institutes of Health Grant AI43474.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Dept. of Microbiology & Immunology, Medical College of Ohio, 3055 Arlington Ave., Toledo, OH 43614-5806. E-mail: mboyle@mco.edu.


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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This article has been cited by other articles:


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Infect. Immun.Home page
M. C. Fontaine, J. J. Lee, and M. A. Kehoe
Combined Contributions of Streptolysin O and Streptolysin S to Virulence of Serotype M5 Streptococcus pyogenes Strain Manfredo
Infect. Immun., July 1, 2003; 71(7): 3857 - 3865.
[Abstract] [Full Text] [PDF]




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