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FEMS Microbiol Lett. 2007 Aug;273(1):96-102. Epub 2007 Jun 6.

Maturation of fimbria precursor protein by exogenous gingipains in Porphyromonas gingivalis gingipain-null mutant.

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1
Department of Oral Frontier Biology, Osaka University Graduate School of Dentistry, Suita-Osaka, Japan.

Abstract

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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