HEMAGGLUTININ ACTIVITY AND HETEROGENEITY OF RELATED PORPHYROMONAS-GINGIVALIS PROTEINASES

Thiol-dependent proteinases that are expressed and released by Porphyr omonas gingivalis are considered virulence factors in periodontitis be cause of their potential to effect matrix degradation and inflammation . A number of P. gingivalis thiol-proteinases have been described, how ever, with similar biochemical characteristics. In this report we demo nstrate that an isolated P. gingivalis proteinase consists of noncoval ently associated peptides and that slight variations in the associatio n pattern of these peptides could result in different proteinases with different affinities and activities. We also describe the co-purifica tion of thiol-proteinase activity with hemagglutinin activity and demo nstrate that each type of activity has similar inhibition profiles. Wi th the use of monoclonal antibodies against the P. gingivalis proteina se we follow proteinase released into the culture medium over the cour se of 10 days and, by Western blot analysis, demonstrate that many of the proteinases with varying molecular weight are related. The identif ication of a single, immunoreactive, 140 kDa proteinase detected early in the culture and in association with the P. gingivalis cells sugges ts that multiple proteinases may originate from a single 140 kDa prote inase.