Hemagglutinin activity and heterogeneity of related Porphyromonas gingivalis proteinases.

Abstract

Thiol-dependent proteinases that are expressed and released by Porphyromonas gingivalis are considered virulence factors in periodontitis because of their potential to effect matrix degradation and inflammation. A number of P. gingivalis thiol-proteinases have been described, however, with similar biochemical characteristics. In this report we demonstrate that an isolate P. gingivalis proteinase consists of noncovalently associated peptides and that slight variations in the association pattern of these peptides could result in different proteinases with different affinities and activities. We also describe the co-purification of thiol-proteinase activity with hemagglutinin activity and demonstrate that each type of activity has similar inhibition profiles. With the use of monoclonal antibodies against the P. gingivalis proteinase we follow proteinase released into the culture medium over the course of 10 days and, by Western blot analysis, demonstrate that many of the proteinases with varying molecular weight are related. The identification of a single, immunoreactive, 140 kDa proteinase detected early in the culture and in association with the P. gingivalis cells suggests that multiple proteinase may originate from a single 140 kDa proteinase.