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Streptococcus pyogenes are important pathogenic
bacteria which produce an extracellular cysteine proteinase
contributing to their virulence and pathogenicity. S. pyogenes also express surface molecules, M proteins, that are major
virulence determinants due to their antiphagocytic property. In the
present work live S. pyogenes bacteria of the M1 serotype were
incubated with purified cysteine proteinase. Several peptides were
solubilized, and analysis of their protein-binding properties and amino
acid sequences revealed two internal fibrinogen-binding fragments of M1
protein (17 and 21 kDa, respectively), and a 36-kDa IgG-binding
NH
Volume 270,
Number 17,
Issue of April 28, pp. 9862-9867, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
-terminal fragment of protein H, an IgGFc-binding surface
molecule. M protein also plays a role in streptococcal adherence, and
removal of this and other surface proteins could promote bacterial
dissemination, whereas the generation of soluble complexes between
immunoglobulins and immunoglobulin-binding streptococcal surface
proteins could be an etiological factor in the development of
glomerulonephritis and rheumatic fever. Thus, in these serious
complications to S. pyogenes infections immune complexes are
found in affected organs. The cysteine proteinase also solubilized a
116-kDa internal fragment of C5a peptidase, another streptococcal
surface protein. Activation of the complement system generates C5a, a
peptide stimulating leukocyte chemotaxis. C5a-mediated granulocyte
migration was blocked by the 116-kDa fragment. This mechanism, by which
phagocytes could be prevented from reaching the site of infection, may
also contribute to the pathogenicity and virulence of S. pyogenes.
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