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J. Biol. Chem., Vol. 277, Issue 15, 12642-12648, April 12, 2002
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From the Department of Medical Microbiology, Dermatology and
Infection, Lund University, Sölvegatan 23, Lund SE-22362, Sweden
The group B streptococcus (GBS) is the most
important cause of life-threatening bacterial infections in newborn
infants. Protective immunity to GBS infection is elicited by several
surface proteins, one of which, the
Streptococcal
Protein Has Separate Binding Sites for Human
Factor H and IgA-Fc*
,
protein, is known to bind human
IgA-Fc. Here, we show that the protein also binds human factor H
(FH), a negative regulator of complement activation. Absorption
experiments with whole human plasma demonstrated binding of FH to a GBS
strain expressing protein but not to an isogenic -negative
mutant. This binding was due to a direct interaction between and
FH, as shown by experiments with purified proteins. Inhibition tests and studies with fragments demonstrated that FH and IgA-Fc bind to
separate and nonoverlapping regions in . Heparin, a known ligand for
FH, specifically inhibited the binding between and FH, suggesting
that FH has overlapping binding sites for and heparin.
Bacteria-bound FH retained its complement regulatory activity, implying
that -expressing GBS may use bound FH to evade complement attack.
The finding that protein binds FH adds to a growing list of
interactions between human pathogens and complement regulatory
proteins, supporting the notion that these interactions are of general
importance in bacterial pathogenesis.
*
This work was supported by Swedish Medical Research Council
Grant 09490 and grants from the Medical Faculty of Lund University, the
Royal Physiographic Society in Lund, the Swedish Society for Medical
Research, and the Trusts of Crafoord, Groschinsky, Hedberg, Jerring, Kock, Lundström, and Österlund.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. Tel.: 46-46-173234;
Fax: 46-46-189117; E-mail: thomas.areschoug@mmb.lu.se.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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