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Porphyromonas gingivalis is a Gram-negative obligate anaerobic bacterium and is considered a keystone pathogen in the initiation of periodontitis, one of the most widespread infectious diseases. Bacterial bis-(3′-5′) cyclic GMP (cyclic di-GMP [c-di-GMP]) serves as a second messenger and is involved in modulating virulence factors in numerous bacteria. However, the role of this second messenger has not been investigated inP. gingivalis , mainly due to a lack of an annotation regarding diguanylate cyclases (DGCs) in this bacterium. Using bioinformatics tools, we found a protein, PGN_1932, containing a GGDEF domain. A deletion mutation in thepgn_1932 gene had a significant effect on the intracellular c-di-GMP level inP. gingivalis . Genetic analysis showed that expression of thefimA andrgpA genes, encoding the major protein subunit of fimbriae and an arginine-specific proteinase, respectively, was downregulated in thepgn_1932 mutant. Correspondingly, FimA protein production and the fimbrial display on the mutant were significantly reduced. Mutations in thepgn_1932 gene also had a significant impact on the adhesive and invasive capabilities ofP. gingivalis , which are required for its pathogenicity. These findings provide evidence that the PGN_1932 protein is both responsible for synthesizing c-di-GMP and involved in biofilm formation and host cell invasion byP. gingivalis by controlling the expression and biosynthesis of FimA.

Identification of a Diguanylate Cyclase and Its Role in Porphyromonas gingivalis Virulence