Enhanced Attachment of Porphyromonas gingivalis to Human Fibroblasts Mediated by Fusobacterium nucleatum

Metzger, Zvi; Blasbalg, Jaron; Dotan, Miri; Weiss, Ervin I.

doi:10.1016/j.joen.2008.10.011

Cited by 29 publications

(25 citation statements)

References 34 publications

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“…Therefore, we also examined the ability of these P. gingivalis strains to adhere to epithelial (HeLa) cells and human periodontal ligament fibroblasts (HPDLFs). Consistent with the observations from previous studies, P. gingivalis strain ATCC 33277 bound to both HPDLFs and HeLa cells (40,41) (Fig. 2B and C).…”

Section: Resultssupporting

confidence: 92%

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

et al. 2014

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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 in P. 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 the pgn_1932 gene had a significant effect on the intracellular c-di-GMP level in P. gingivalis. Genetic analysis showed that expression of the fimA and rgpA genes, encoding the major protein subunit of fimbriae and an arginine-specific proteinase, respectively, was downregulated in the pgn_1932 mutant. Correspondingly, FimA protein production and the fimbrial display on the mutant were significantly reduced. Mutations in the pgn_1932 gene also had a significant impact on the adhesive and invasive capabilities of P. 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 by P. gingivalis by controlling the expression and biosynthesis of FimA.

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Section: Resultssupporting

confidence: 92%

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

et al. 2014

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“…In co‐infection with F nucleatum , the adhesion of P gingivalis was increased in WT cells consistent with the augmented adhesion efficiency of P gingivalis to a human epithelial cell line (CA9‐22) in the presence of F nucleatum shown by others . The same pattern was also observed in human periodontal ligament fibroblasts . Furthermore, in a previous study in our laboratory, we showed that non capsulated P gingivalis (similar to the strain used in the current study) binds better to murine primary keratinocytes in co‐infection with F nucleatum .…”

Section: Discussionsupporting

confidence: 90%

Myd88 plays a major role in the keratinocyte response to infection with Porphyromonas gingivalis

Polak

Zigron

Eli-Berchoer

et al. 2019

J of Periodontal Research

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Aim To explore the role of keratinocyte myeloid differentiation primary response 88 (MyD88) expression in the adhesion of Porphyromonas gingivalis to the cells and its subsequent invasion and intracellular survival. Materials and Methods Primary mouse keratinocytes from wild‐type (WT) or Myd88−/− mice were infected with P gingivalis alone or co‐infected with Fusobacterium nucleatum. Bacterial adhesion and invasion were measured using fluorescent microscopy and flow cytometry, and intracellular survival in keratinocytes was quantified by an antibiotic protection assay. Keratinocyte expression of antimicrobial peptides was measured by real‐time PCR. Results In the absence of MyD88, P gingivalis adherence, invasion, and intracellular survival were enhanced compared with WT keratinocytes. The presence of F nucleatum during infection increased the adhesion of P gingivalis to WT keratinocytes but reduced the adhesion to Myd88−/− keratinocytes. Fusobacterium nucleatum improved mildly the invasion and survival of P gingivalis in both cell types. Baseline expression of beta‐defensin 2, 3, 4 and RegIII‐γ was elevated in Myd88−/− keratinocytes compared to WT cells; however, following infection beta‐defensin expression was strongly induced in WT cells but decreased dramatically in the MyD88 deficient cells. Conclusion In the absence of MyD88 expression, P gingivalis adhesion to keratinocytes is improved, and invasion and intracellular survival are increased. Furthermore, keratinocyte infection by P gingivalis induces antimicrobial peptide expression in a MyD88‐dependent manner. Thus, MyD88 plays a key role in the interaction between P gingivalis and keratinocytes.

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“…1). 26,27 Without F. nucleatum, the number of obligate anaerobic species would decrease sharply in the oral cavity. 28 Some bacterial species can help other species survive by depleting acid and improving the local environment.…”

Section: O N O T D I S T R I B U T Ementioning

confidence: 99%

Bacterial interactions in dental biofilm

2011

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Enhanced Attachment of Porphyromonas gingivalis to Human Fibroblasts Mediated by Fusobacterium nucleatum

Cited by 29 publications

References 34 publications

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

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

Myd88 plays a major role in the keratinocyte response to infection with Porphyromonas gingivalis

Bacterial interactions in dental biofilm

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