Enterococcus faecalis Adhesin, Ace, Mediates Attachment to Particulate Dentin

An enzyme linked immunosorbent assay was developed to assess E. faecalis adhesion to particulate dentin. E. faecalis, OG1RF, which expresses the collagen binding protein (Ace+), and a derivative of OG1RF, TX5256, deficient in the collagen binding protein (Ace−) were grown at 46° C, necessary for in vitro expression of Ace, and at 37° C. E. faecalis binding to dentin was measured at 0, 15, 30, 60, 120, and 360 minutes. Compared to TX5256 and OG1RF grown at 37° C, OG1RF grown at 46° C adhered significantly better at all time points except 15 minutes (p < 0.001) exhibiting maximum binding at 120 minutes (17.4% of a positive control). Type I collagen at 100 μg/ml inhibited dentin binding by OG1RF grown at 46° C in both competition (p < 0.005) and displacement assays (p < 0.046). Immunoaffinity purified anti-Ace IgG at 200 μg of protein inhibited adhesion of OG1RF grown at 46° C to dentin.