Multiple colonization defects in a cysteine protease mutant of Porphyromonas gingivalis.

A cysteine protease mutant, G-102, of Porphyromonas gingivalis 381 defective in the rgp-1 gene has been recently constructed in this laboratory. In order to evaluate the role of the protease in the virulence properties of P. gingivalis, a number of putative periodontopathic properties of the mutant were evaluated. Relative to the parental strain, mutant G-102 was demonstrated to be defective in interacting with Gram-positive bacteria as well as cultured epithelial cells. In addition, the mutant was altered in attaching to the protein components of extracellular matrix as well as to type I collagen. Some of these alterations could result from the decreased autoaggregation displayed by mutant G-102 relative to strain 381. However, since the epithelial cell attachment assays were carried out at very low bacterial densities, it is unlikely that reduced autoaggregation of the mutant is responsible for its decreased ability to attach to these eucaryotic cells. Electron microscopic examination of the cells also revealed that mutant G-102 was altered in normal fimbrae expression. In addition, reduced expression of the 43 kDa fimbrial subunit in the mutant was detected with both Western and Northern blotting. These results indicated that the rgp-1 gene product can play either a direct or indirect role in the colonization properties of P. gingivalis.