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2007:
Kato Takahiro; Tsuda Tetsuhisa; Omori Hiroko; Kato Takafumi; Yoshimori Tamotsu; Amano Atsuo
Maturation of fimbria precursor protein by exogenous gingipains in Porphyromonas gingivalis gingipain-null mutant.
FEMS microbiology letters 2007;
273(
1):.
Porphyromonas gingivalis expresses several virulence factors such as fimbriae and proteases, termed gingipains, which are enzymes that process precursor fimbriae proteins. Thus, gingipain-null mutants lack mature fimbriae. Membrane vesicle-depleted supernatants (VDS) containing soluble gingipains were prepared as an exogenous gingipain fraction. Precursor proteins were treated with VDS and a fimbriated gingipain-null mutant was successfully generated. Experiments showed that the wild strain adhered to and invaded epithelial cells at a greater level than the fimbriated gingipain-null mutant, while adhesion/invasion was prevented in the presence of fetal calf serum, which inhibits gingipain activity. The findings of this study suggest that gingipains expose cellular cryptic ligands in a proteolytic manner and promote fimbriae binding to epithelial cells.
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