Recent clinical studies showed that B. forsythus was significantly associated with advanced periodontitis and recurrent periodontitis. Although B. forsythus has been implicated in the pathogenesis of periodontal disease, its role as a pathogen remains unclear. It has been demonstrated that acidic proline-rich proteins (PRPS) are the salivary receptors for many bacteria such as streptococcus gordonii, streptococcus sanguis,Actinomyces naeslundii, porphyromonas gingivalis. Therefore, we hypothesized that PRPS was also the salivary receptors of B. forsythus adhesins which mediated B. forsythus adherence to the oral surfaces. Objective: to confirm our assumption, we focused on identifying surface adhesins of B. forsythus which interact with human salivary proline-rich proteins (PRPS). Methods: Proteins of B. forsythus separated by SDS-PAGE were transferred to polyvinylidene difluoride membranes by using a semidry transfer system, and the unoccupied sites were blocked by incubating the membrane at 4C overnight with 5% skim milk TBS (1.37M NaCl, 27mMKCl, 81mM Na2HPO4.12H2O, 15mM KH2PO4, PH 7.4). The membranes were then incubated with biotin-labeled human salivary PRP for 1 hour at room temperature and washed with PBS. The bound proteins were detected by incubating the membrane with detection solution for 1 minute at room temperature after the membrane was incubated with streptavidin in HRP diluted 1:1500 by PBS for 1 hour at room temperature, and recorded with X-ray film by autoradiography. Results: PRPS interacted with 85 Kda, 65 Kda, 60 Kda, 49Kda protein bands from B. forsythus separated with SDS-PAGE. Conclusions: These results indicated that these proteins were likely to be adhesins of B. forsythus and PRPS were specific salivary receptors of these adhesins.

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