Concentration-dependent effect of fibrinogen on IgG-specific antigen binding and phagocytosis.

In this paper, we aim to characterize fibrinogen-IgG interactions, and explore how fibrinogen alters IgG-mediated phagocytosis. Using enzyme-linked binding assays, we found that fibrinogen binding to IgG is optimized for surfaces coated with high levels of IgG. Using a similar method, we have shown that for an antigen unable to specifically bind fibrinogen, fibrinogen enhances binding of antibodies towards that antigen.

Fibrinogen binds IgG antibody and enhances IgG-mediated phagocytosis.

While Fibrinogen (Fg) and Immunoglobulin G (IgG) are traditionally thought to have separate functions in thrombosis and immune response, recent studies suggest overlapping functions. Here we present evidence that Fibrinogen binds to IgG specifically, and that Fibrinogen-IgG interactions enhance phagocytosis. We demonstrate specific, saturable binding of Fibrinogen to immobilized IgG and its fragments on nitrocellulose or poly-(L)-Lys styrene plates using Biotin/Streptavidin-Horse Radish Peroxidase detection systems.

Intracellular signaling and cytokine induction upon interactions of Porphyromonas gingivalis fimbriae with pattern-recognition receptors.

Toll-like receptors (TLRs) and other pattern-recognition receptors (PRRs) of the innate immune system form functional receptor complexes that recognize and respond to pathogen-associated molecular patterns (PAMPs). Porphyromonas gingivalis is an important pathogen in human periodontitis and has also been implicated in atherosclerosis. A major virulence factor of this pathogen is the fimbriae, which function as a surface adhesin.

Dependence of bacterial protein adhesins on toll-like receptors for proinflammatory cytokine induction.

Toll-like receptors (TLRs) are important signal transducers that mediate inflammatory reactions induced by microbes through pattern recognition of virulence molecules such as lipopolysaccharide (LPS) and lipoproteins. We investigated whether proinflammatory cytokine responses induced by certain bacterial protein adhesins may also depend on TLRs. In differentiated THP-1 mononuclear cells stimulated by LPS-free recombinant fimbrillin (rFimA) from Porphyromonas gingivalis, cytokine release was abrogated by monoclonal antibodies (MAbs) to CD14 and TLR4 but not to TLR2.