Role of Porphyromonas gingivalis protease activity in colonization of oral surfaces.
Cysteine proteases, including Arg-gingipain of Porphyromonas gingivalis, have been implicated as important virulence factors in periodontal diseases. These enzymes are also involved in the hemagglutinating activity of the organisms. In order to determine the role of proteases in the colonization of the gingival margin, we have compared the attachment properties of P. gingivalis 381 with those of its Arg-gingipain-defective mutant, G-102. Interactions with gram-positive bacteria, human oral epithelial cells, extracellular matrix proteins, and type I collagen were evaluated. In all cases, mutant G-102 was deficient in attachment relative to the parental strain. The mutant's defects could be explained, in part, by the weak autoaggregation displayed by the mutant, which appeared to result from altered fimbrial expression. Both Western blot (immunoblot) and Northern (RNA) blot analyses indicated reduced expression of the major 43-kDa fimbrillin subunit in the mutant. These results suggest that Arg-gingipain may play both direct and indirect roles in the colonization of the gingival margin. In addition, fimbriae may play a direct role in interacting with some host surfaces.
Tokuda
M
M
Department of Oral Biology, State University of New York at Buffalo, 14214, USA.
Duncan
M
M
Cho
M I
MI
Kuramitsu
H K
HK
D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000032:analysis; D003546:Cysteine Endopeptidases / Q000502:physiology*; D036781:Fimbriae Proteins; D006801:Humans; D007624:KB Cells; D009055:Mouth / Q000382:microbiology*; D009154:Mutation; D016966:Porphyromonas gingivalis / Q000201:enzymology* / Q000472:pathogenicity; D014774:Virulence
D001426:Bacterial Proteins; C063055:fimbrillin; D036781:Fimbriae Proteins; D003546:Cysteine Endopeptidases