Porphyromonas gingivalis fimbriae are pro-inflammatory but do not play a prominent role in the innate immune response to P. gingivalis.

The fimA gene encodes the major fimbrial protein of Porphyromonas gingivalis. It has been shown to stimulate adhesion to salivary proteins and other bacteria. It is also thought to play a major role in invading and stimulating host cells. To determine whether the fimA gene represents one of the principal molecules of P. gingivalis that induces inflammation, we tested purified FimA protein and a mutant P. gingivalis (DPG3) that lacks the fimA gene versus wild-type (WT) P. gingivalis. When injected into connective tissue of the scalp, purified FimA protein induced TNF-alpha and MIP-2 expression confirming that it is pro-inflammatory. WT P. gingivalis induced TNF-alpha expression and recruitment of PMNs in the same model. However, DPG3 P. gingivalis stimulated TNF expression and PMN recruitment to the same extent. The latter was consistent with similar induction of the chemokine MIP-2. Similar results were obtained with diabetic mice that have a more prolonged inflammatory response to bacterial stimulation. These results indicate that FimA is a potent inducer of inflammatory cytokine expression but, in the context of P. gingivalis infection, it is not a principal stimulator of the innate host response.