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(Received for publication, April 21, 1997, and in revised form, May 30, 1997)
From the Departments of Protein H, a surface protein of
Streptococcus pyogenes interacting with the constant Fc
region of IgG, is known to be released from the streptococcal surface
by a cysteine proteinase produced by the bacteria. Poststreptococcal
glomerulonephritis and rheumatic fever are conditions in which immune
complexes and autoimmune mechanisms have been suggested to play
pathogenetic roles. The present study demonstrates that addition of
protein H to human serum produces complement activation with
dose-dependent cleavage of C3. The activation was
IgG-dependent and the result of complexes formed between
IgG and protein H. These complexes were size heterogeneous with
molecular masses of 400 kDa to 1.4 MDa. Using complement-depleted serum
reconstituted with complement proteins, the activation by protein H was
found to be dependent of the classical, but independent of the
alternative pathway of complement. In contrast to results of
experiments based on soluble protein H·IgG complexes, complement activation was inhibited by protein H when IgG was immobilized on a
surface. The interaction between C1q and immunoglobulins represents the
first step in the activation of the classical pathway, and protein H
efficiently inhibited the binding of C1q to IgG immobilized on
polyacrylamide beads. Protein H reduced C3 deposition on the IgG-coated
beads and inhibited immune hemolysis of IgG-sensitized erythrocytes.
Finally, significantly less C3 was deposited on the surface of protein
H-expressing wild-type streptococci than on the surface of isogenic
mutant bacteria devoid of protein H. The results demonstrate that
protein H·IgG complexes released from the streptococcal surface can
produce complement breakdown at the sites of infection, whereas
complement activation on bacterial surfaces is inhibited. This should
have important implications for host-parasite relationships. In
addition, soluble protein H·IgG complexes might contribute to
immunological complications of streptococcal infections.
Volume 272, Number 33,
Issue of August 15, 1997
pp. 20774-20781
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
Cell and Molecular Biology
and ¶ Medical Microbiology, Lund University, S-221 00 Lund, Sweden
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