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Infection and Immunity, July 2003, p. 3740-3747, Vol. 71, No. 7
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.7.3740-3747.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Gingipain RgpB Is Excreted as a Proenzyme in the vimA-Defective Mutant Porphyromonas gingivalis FLL92

G. Jon Olango,1 Francis Roy,1 Shaun M. Sheets,1 Mary K. Young,2 and Hansel M. Fletcher1*

Division of Microbiology and Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda, California 92350,1 Division of Immunology, Beckman Research Institute of the City of Hope, Duarte, California 910102

Received 18 September 2002/ Returned for modification 16 December 2002/ Accepted 25 March 2003

We have previously shown that the unique vimA (virulence-modulating) gene could modulate proteolytic activity in Porphyromomas gingivalis. Although a reduction in cysteine protease activity was observed in the vimA-defective mutant, P. gingivalis FLL92, compared to that of the wild-type strain, no changes were seen in the expression of the gingipain genes. This result might suggest posttranscriptional regulation of protease expression. To determine whether there was a defect in the translation, transport, or maturation of the gingipains, P. gingivalis FLL92 was further characterized. In contrast to the wild-type strain, a 90% reduction was seen in both Rgp and Kgp protease activities in strain FLL92 during the exponential growth phase. These activities, however, increased to approximately 60% of that of the wild-type strain during stationary phase. Throughout all the growth phases, Rgp and Kgp activities were mostly soluble, in contrast to those of the wild-type strain. Western blot analyses identified unique Rgp- and Kgp-immunoreactive bands in extracellular protein fractions from FLL92 grown to late exponential phase. Also, the RgpB proenzyme was identified in this fraction by mass spectrometry. In addition, in vitro protease activity could be induced by a urea denaturation-renaturation cycle in this fraction. These results indicate that protease activity in P. gingivalis may be growth phase regulated, possibly by multiple mechanisms. Furthermore, the gingipain RgpB is excreted in an inactive form in the vimA mutant. In addition, these results provide the first evidence of posttranslational regulation of protease activity in P. gingivalis and may suggest an important role for the vimA gene in protease activation in this organism.

* Corresponding author. Mailing address: Division of Microbiology and Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda, CA 92350. Phone: (909) 558-1000. Fax: (909) 558-4035. E-mail: hfletcher{at}som.llu.edu.

Editor: V. J. DiRita

Infection and Immunity, July 2003, p. 3740-3747, Vol. 71, No. 7
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.7.3740-3747.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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