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J. Biol. Chem., Vol. 276, Issue 45, 41790-41796, November 9, 2001
From the 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.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc. This article has been cited by other articles:
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