Porphyromonas gingivalis and Tannerella forsythia have been implicated as the major etiologic agents of periodontal disease. These two bacteria are frequently isolated together from the periodontal lesion, and it has been suggested that their interaction may increase each one’s virulence potential. The purpose of this study was to identify proteins on the surface of these organisms that are involved in interbacterial binding.

Biotin labeling of surface proteins of P. gingivalis and T. forsythia and liquid chromatography–tandem mass spectrometry (LC-MS/MS) analysis was performed to identify surface proteins involved in the coaggregating activity between P. gingivalis and T. forsythia.

It was found that three major T. forsythia proteins sized 161, 100, and 62 kDa were involved in binding to P. gingivalis , and P. gingivalis proteins sized 35, 32, and 26 kDa were involved in binding to T. forsythia cells.

LC-MS/MS analysis identified one T. forsythia surface protein (TonB-linked outer membrane protein) involved in interbacterial binding to P. gingivalis . However, the nature of other T. forsythia and P. gingivalis surface proteins identified by biotin labeling could not be determined. Further analysis of these proteins will help elucidate the molecular mechanisms that mediate coaggregation between P. gingivalis and T. forsythia.