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Infection and Immunity, December 2000, p. 6574-6579, Vol. 68, No. 12
School of Dentistry, Meharry Medical College,
Nashville, Tennessee,1 and Department
of Oral Biology, University of Washington, Seattle,
Washington2
Received 25 May 2000/Returned for modification 1 August
2000/Accepted 7 September 2000
In common with many bacterial virulence genes, the fimbrillin
(fimA) gene of Porphyromonas gingivalis is
modulated in response to environmental fluctuation. The
trans-acting components that comprise the regulatory system
for transcriptional activity of the fimA gene in
P. gingivalis were investigated. Three major proteins
were found to bind to the upstream region of the fimA promoter. One of these proteins was fimbrillin itself, and the other two were a major arginine protease (Rgp) and lysine
protease (Kgp). Production of these proteins was necessary
for maximal fimA transcription. An exogenous
fimA promoter-lacZ reporter was inactive when
introduced into a strain of P. gingivalis carrying a
mutation in the indigenous fimA gene. Furthermore,
fimA mRNA levels were significantly decreased in
rgp and kgp mutant strains. These data indicate
that P. gingivalis has evolved multiple levels of
control of fimbrial gene expression to enhance its survival in hostile environments.
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Regulation of the Porphyromonas gingivalis fimA
(Fimbrillin) Gene
*
Corresponding author. Mailing address: School of
Dentistry, Meharry Medical College, Nashville, TN 37208. Phone: (615)
327-5981. Fax: (615) 327-2989. E-mail:
hxie{at}mail.mmc.edu.
Infection and Immunity, December 2000, p. 6574-6579, Vol. 68, No. 12
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
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