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J Biol Chem, Vol. 273, Issue 44, 29072-29076, October 30, 1998
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From the Departments of Arg-gingipain (RGP) is an
Arg-X-specific cysteine proteinase produced by the
Gram-negative anaerobe Porphyromonas gingivalis and has
been shown to be a potent virulence factor in progressive periodontal
disease (Nakayama, K., Kadowaki, T., Okamoto, K., and Yamamoto, K. (1995) J. Biol. Chem. 270, 23619-23626). In this study, we provide evidence that RGP acts as a major processing enzyme
for various cell surface and secretory proteins in P. gingivalis. Fimbrilin, a major component of fimbriae, remained in
the precursor form in the RGP-null mutant. Prefimbrilin expressed in
Escherichia coli was converted to the mature fimbrilin
in vitro when incubated with purified RGP, but its
conversion was suppressed by potent RGP inhibitors. The results were
consistent with the electron microscopic observation indicating little
or no fimbriation in the RGP-null mutant. The immunogenic 75-kDa cell
surface protein was also shown to retain its proform in the RGP-null
mutant. In addition, Lys-gingipain (KGP) was found to be abnormally
processed in the RGP-null mutant. In contrast, both prefimbrilin and
the 75-kDa protein precursor were processed to their respective mature forms in the KGP-null mutant, suggesting that KGP is not involved in
the normal processing mechanisms of these proteins. These results suggest that RGP not only acts as a direct virulence factor but also
makes a significant contribution as a major processing enzyme to the
virulence of P. gingivalis.
Pharmacology and
¶ Microbiology, Kyushu University Faculty of Dentistry, Fukuoka
812-8582, Japan and the Department of Microbiology, School of
Dentistry, Aichi-Gakuin University, Nagoya 464-8650, Japan
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