Anti-bacterial efficacy of new self-etching dentine bonding agent.

Since a perfect seal is not easily achieved during bonding procedures, any product which will limit or delay bacterial proliferation in the resulting micro-leakage spaces should extend the life span of bonded restorations. This study compared the antibacterial properties of an experimental, self-etching, fluoride-releasing, antibacterial bonding system (ABF) with two standard bonding systems (SE Bond and Scotchbond MP). Spread plates of three different bacteria (Streptococcus mutans, Lactobacillus paracasei and Actinomyces naeslundii) were prepared on Brain-Heart Infusion agar. Standardised, sterilised filtration paper disks were infiltrated with 20 microl of primer and then placed on the inoculated agar and incubated at 37 degrees C for 48 hours. The extent of the inhibition zones were measured at different positions and data were analysed using the Student t-test to determine significant differences. All three primers showed zones of inhibition for all three bacteria tested. Inhibition zones for ABF primer against S. mutans were significantly larger (p<0.05) compared to that of Scotchbond MP and SE Bond. In general the antibacterial activity of the three primers against the three bacteria tested varied, and the inhibitory effect for the experimental primer was significantly superior against S. mutans only.

Identification of phosphatidylinositol mannoside as a mycobacterial adhesin mediating both direct and opsonic binding to nonphagocytic mammalian cells.

The molecular basis for the binding of Mycobacterium tuberculosis to nonphagocytic cells, which are readily infected in vitro, and the in vivo significance of this interaction are incompletely understood. Of six cell types tested, we found that only two, Chinese hamster ovary (CHO) fibroblasts and primary porcine aortic endothelial cells, were able to bind M. tuberculosis H37Rv efficiently in vitro. Binding to both CHO and endothelial cells was markedly (three- to fivefold) enhanced by 10 to 20% human or bovine serum, suggesting that the bacteria were coated by a serum opsonin. Preincubation with individual candidate opsonins revealed that recombinant human mannose-binding protein (rMBP), fibronectin, and transferrin were each able to enhance binding threefold. Preincubation of bacteria in serum depleted of mannan-binding lectins or in genetic MBP-deficient serum resulted in enhancements that were only approximately 60 and 58%, respectively, of that produced by preincubation in control serum. In contrast, serum depleted of fibronectin or transferrin retained its opsonizing capacity, suggesting that the latter two are not significant opsonins in whole serum. Binding of M. tuberculosis and Mycobacterium smegmatis to both CHO and endothelial cells in the presence or absence of serum was blocked (60 to 70%) by a monoclonal antibody, MAb 1D1, selected for recognition of intact bacilli. The 1D1 antigen was purified from mycobacterial cell walls and chemically identified as a polar phosphatidylinositol mannoside (PIM). Latex beads coated with purified 1D1 antigen bound to CHO cells, which was enhanced threefold by serum and abolished by periodate treatment, suggesting a requirement for the PIM mannoses in opsonic adhesion. This was likely mediated, at least in part, by serum MBP, as rMBP bound strongly to 1D1 antigen in both thin-layer chromatography overlay and plate binding assays, the latter in a mannan-inhibitable manner. This is the first demonstration that mycobacterial PIMs can function as adhesins for binding to nonphagocytic cells, both directly and after opsonization with serum proteins, including MBP.