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*
Department of Clinical Chemistry, Lund University, University Hospital Malmö, Malmö, Sweden;
Laboratory for Bacteriology, Microbiology and Tumor Biology Center, Karolinska Institute, Stockholm, Sweden; and
Department of Laboratory Medicine, Lund University, Lund, Sweden
C4b-binding protein (C4BP) is an important plasma inhibitor of the
classical pathway of complement activation. Several bacterial pathogens
bind C4BP, which may contribute to their virulence. In the present
report we demonstrate that isolated type IV pili from Neisseria
gonorrhoeae bind human C4BP in a dose-dependent and saturable
manner. C4BP consists of seven identical 
-chains and one 
-chain
linked together with disulfide bridges. We found that pili bind to the
-chain of C4BP, which is composed of eight homologous complement
control protein (CCP) domains. From the results of an inhibition assay
with C4b and a competition assay in which we tested mutants of C4BP
lacking individual CCPs, we concluded that the binding area for pili is
localized to CCP1 and CCP2 of the -chain. The binding between pili
and C4BP was abolished at 0.25 M NaCl, implying that it is based mostly
on ionic interactions, similarly to what have been observed for
C4b-C4BP binding. Furthermore, the N-terminal part of PilC, a
structural component of pili, appeared to be responsible for binding of
C4BP. Membrane cofactor protein, previously shown to be a receptor for
pathogenic N. gonorrhoeae on the surface of epithelial
cells, competed with C4BP for binding to pili only at high
concentrations, suggesting that different parts of pili are involved in
these two interactions. Accordingly, high concentrations of C4BP were
required to inhibit binding of N. gonorrhoeae to Chang
conjunctiva cells, and no inhibition of binding was observed with
cervical epithelial cells.
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