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J. Biol. Chem., Vol. 278, Issue 19, 16561-16566, May 9, 2003
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§,
,
From the Some isolates of the significant human pathogen
Streptococcus pyogenes, including virulent strains of the
M1 serotype, secrete protein SIC. This molecule, secreted in large
quantities, interferes with complement function. As a result of natural
selection, SIC shows a high degree of variation. Here we provide a
plausible explanation for this variation and the fact that strains of
the M1 serotype are the most frequent cause of severe invasive S. pyogenes infections. Thus, protein SIC was found to inactivate human neutrophil
Section for Molecular Pathogenesis,
Department of Cell and Molecular Biology, Lund University, and
the ¶ Department of Medical Microbiology, Dermatology, and
Infection, Lund University Hospital, S-221 85 Lund,
Sweden
-defensin and LL-37, two major antibacterial peptides involved in bacterial clearance. This inactivation protected S. pyogenes against the antibacterial effect of the
peptides. Moreover, SIC isolated from S. pyogenes of the M1
serotype was more powerful in this respect than SIC variants from
strains of M serotypes 12 and 55, serotypes rarely connected with
invasive infections.
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