1 C4bp alpha-chain monomers did not bind gonococci, indica
2 C4bp contains seven identical alpha-chains and one beta-
3 C4bp-Por1B interactions were ionic in nature (inhibited
4 Using fAb fragments
against C4bp SCR1, C4bp binding to Por1A and Por1B strains was i
5 gesting a novel interaction between OmpA
and C4bp.
6 ly described adjuvant IMX313, a hybrid
avian C4bp oligomerization domain, could increase T cell respo
7 Microbial surface-
bound C4bp demonstrated cofactor activity.
8 nococci together formed a negatively
charged C4bp-binding domain.
9 Por1B gonococci bound
chimpanzee C4bp and resisted killing by chimpanzee serum, providing
10 wed that the loop 1 of Por1A is required
for C4bp binding.
11 onococci was restored in these sera by
human C4bp.
12 nding to CCP3 sequences block the binding
of C4bp to OmpA and also significantly enhance serum bacter
13 Binding
of C4bp to OmpA is not significantly inhibited in the prese
14 We found that OmpA binds the alpha-chain
of C4bp, which is composed of eight homologous complement c
15 cocci, indicating that the polymeric form
of C4bp was required for binding.
16 normal serum, underscoring the importance
of C4bp in mediating gonococcal serum resistance.
17 down-regulatory protein C4b-binding
protein (
C4bp) to evade killing by human complement.
18 esistance by binding to C4b binding
protein (
C4bp), a complement fluid phase regulator.
19 e complement regulator, C4b-binding
protein (
C4bp).
20 Binding studies using mutants of
recombinant C4bp that lack one CCP at a time suggest that CCP3 is th
21 Only
recombinant C4bp mutant molecules containing the NH2-terminal alpha-
22 Using fAb fragments against C4bp
SCR1,
C4bp binding to Por1A and Por1B strains was inhibited in
23 irtually all mammals, bound species-
specific C4bp and uniformly resisted serum complement-mediated ki
24 ted by high salt or by heparin), whereas
the C4bp-Por1A bond was hydrophobic.
25 experimentally with this organism and
whose C4bp molecules did not bind to N. gonorrhoeae.
26 e that the N terminus of OmpA interacts
with C4bp.