MOLECULAR-CLONING AND STRUCTURAL CHARACTERIZATION OF THE ARG-GINGIPAIN PROTEINASE OF PORPHYROMONAS-GINGIVALIS - BIOSYNTHESIS AS A PROTEINASE-ADHESIN POLYPROTEIN

The identification of proteinases of Porphyromonas gingivalis that act as virulence factors in periodontal disease has important implication s in the study of host-pathogen interactions as well as in the discove ry of potential therapeutic and immunoprophylactic agents. We have clo ned and characterized a gene that encodes the 50-kDa cysteine proteina se gingipain or Arg-gingipain-1 (RGP-1) described previously (Chen, Z. , Potempa, J., Polanowski, A., Wikstrom, M., and Travis, J. (1992) J. Biol. Chem,.267, 18896-18901). Analysis of the amino acid sequence of RGP-1 deduced from the cloned DNA sequence showed that the biosynthesi s of this proteinase involves processing of a polyprotein that contain s multiple adhesin molecules located at its carboxyl terminus, This fi nding corroborates previous evidence (Pike R., McGraw, W., Potempa, J. , and Travis, J. (1994) J. Biol. Chem. 269, 406-411) that RGP-1 is clo sely associated with adhesin molecules, and that high molecular weight forms of the proteinase are involved in the binding of erythrocytes.