Comparison of pathogenic properties between two types of arginine-specific cysteine proteinases (gingipains-R) from Porphyromonas gingivalis.

Two major arginine-specific cysteine proteinases (gingipains R) from Porphyromonas gingivalis have been compared with regard to their potential participation in the pathology of periodontal disease. Both the high and low molecular mass forms, HRgpA and RgpB, cleaved oligopeptide fluorogenic substrates at the P1-arginine residue with essentially identical specificity but different efficiencies, with HRgpA being about 1.5 to seven-fold less potent than RgpB. In contrast HRgpA, which occurs as a non-covalent complex of catalytic and hemagglutinin/adhesion domains, was about two-fold more active than RgpB in degrading fibrinogen and fibrin, while both enzymes activated prekallikrein with similar efficiency. These data indicate the likelihood that both activities could be involved in both the bleeding tendency and production of gingival crevicular fluid, which occur at infected periodontitis sites. Significantly, however, is the fact that HRgpA, but not RgpB, was able to bind phospholipids in the presence of calcium ions, the effect dramatically enhancing the activation of clotting factors by this proteinase. This suggests that HRgpA may play a more important role in the virulence of Porphyromonas gingivalis, relative to RgpB, almost certainly because of the presence of the hemagglutinin/adhesion domain which can bind phospholipid and apparently modulate enzyme activity. Copyright 2000 Academic Press.