Variations of <i>Porphyromonas gingivalis</i> fimbriae in relation to microbial pathogenesis

Amano, Atsuo; Nakagawa, Ichirô; Okahashi, Nobuo; Hamada, Naoki

doi:10.1111/j.1600-0765.2004.00719.x

Cited by 213 publications

(237 citation statements)

References 69 publications

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“…This adherence ability is important for bacterial colonization and is driven predominantly by peritrichous fimbriae. Two distinct fimbriae are present on the surface of P. gingivalis cells (1). Major fimbriae are long, peritrichous, filamentous components.…”

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confidence: 99%

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Porphyromonas gingivalis Minor Fimbriae Are Required for Cell-Cell Interactions

Lin

Xie

2006

Infect Immun

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confidence: 99%

“…A thin, short secondary fimbrial structure, termed minor fimbriae or short fimbriae (15), is composed of a 67-kDa protein encoded by the mfa1 gene (4). Both major and minor fimbriae appear to contribute to the pathogenicity of P. gingivalis (1). The primary role of FimA is to promote bacterial attachment to oral surfaces.…”

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confidence: 99%

Porphyromonas gingivalis Minor Fimbriae Are Required for Cell-Cell Interactions

Lin

Xie

2006

Infect Immun

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“…Within the oral biofilm community, the release of ammonia from this first reaction plays an important role in inhibiting tooth decay and in modulating the microbial composition of the community through neutralization of acid end products that are produced by a variety of oral bacteria via fermentation of sugars (Burne & Marquis, 2000;Casiano-Coló n & Marquis, 1988; Nascimento et al, 2009). In contrast with its canonical role in anaerobic ATP synthesis within the cytoplasm, ADI's function as an extracellular enzyme is unclear.Our studies have shown that exposure of P. gingivalis strain 381 to ADI secreted by S. intermedius results in a decrease in the expression of fimbrial subunits (encoded by fimA and mfa1), which are both key virulence determinants and essential to biofilm development (Amano et al, 2004;Christopher et al, 2010; Hamada et al, 1998;Lamont & Jenkinson, 1998;Xie et al, 2007). This interspecies inhibition is consistent with reports by Xie and colleagues that showed the effect of a cell-wall-associated Streptococcus cristatus arginine deiminase on P. gingivalis strain 33277, with the only distinction being that in strain 33277 expression of fimA, but not mfa1, is altered (Wu & Xie, 2010;Xie et al, 2007).…”

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Arginine deiminase inhibits Porphyromonas gingivalis surface attachment

Cugini

Stephens²,

Nguyen³

et al. 2013

Microbiology

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The oral cavity is host to a complex microbial community whose maintenance depends on an array of cell-to-cell interactions and communication networks, with little known regarding the nature of the signals or mechanisms by which they are sensed and transmitted. Determining the signals that control attachment, biofilm development and outgrowth of oral pathogens is fundamental to understanding pathogenic biofilm development. We have previously identified a secreted arginine deiminase (ADI) produced by Streptococcus intermedius that inhibited biofilm development of the commensal pathogen Porphyromonas gingivalis through downregulation of genes encoding the major (fimA) and minor (mfa1) fimbriae, both of which are required for proper biofilm development. Here we report that this inhibitory effect is dependent on enzymic activity. We have successfully cloned, expressed and defined the conditions to ensure that ADI from S. intermedius is enzymically active. Along with the cloning of the wild-type allele, we have created a catalytic mutant (ADIC399S), in which the resulting protein is not able to catalyse the hydrolysis of L-arginine to L-citrulline. P. gingivalis is insensitive to the ADIC399S catalytic mutant, demonstrating that enzymic activity is required for the effects of ADI on biofilm formation. Biofilm formation is absent under L-arginine-deplete conditions, and can be recovered by the addition of the amino acid. Taken together, the results indicate that arginine is an important signal that directs biofilm formation by this anaerobe. Based on our findings, we postulate that ADI functions to reduce arginine levels and, by a yet to be identified mechanism, signals P. gingivalis to alter biofilm development. ADI release from the streptococcal cell and its cross-genera effects are important findings in understanding the nature of inter-bacterial signalling and biofilm-mediated diseases of the oral cavity. INTRODUCTIONPorphyromonas gingivalis is an oral pathobiont, i.e. a natural member of the human microbiota, that under certain perturbations to the host and/or microflora can cause pathology. This Gram-negative, highly proteolytic anaerobe is regarded as the primary aetiological agent of adult periodontal disease, leading to chronic inflammation and destruction of both the soft and hard tissues supporting the teeth (Choil et al., 1990;Dzink et al., 1988; Grossi et al., 1994;Lamont & Jenkinson, 2000;Moore et al., 1991). As a pathobiont, the ability to proliferate and express virulence determinants is central to its shift to pathogenicity, thus determining the mechanisms that control the emergence of its pathogenic state are of fundamental importance.P. gingivalis is a strict anaerobe that preferentially utilizes protein or peptide substrates for growth. Although studies have shown that P. gingivalis may utilize free amino acids or dipeptides, the uptake and growth rates on these substrates are limited and highly variable among strains (Seddon et al., 1988;Takahashi et al., 2000;Tang-Larsen et al., 1995). In general...

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“…P. gingivalis enters gingival epithelial cells by endocytosis, which mediates binding of Rgp to the cells [22]. It must be noted that gingipains are required for maturation of P. gingivalis fimbriae [23], which is essential for internalization of the bacterium into epithelial cells [24]. However, endocytosis of both PAR-2 and P. gingivalis are probably required for the up-regulation of IL-33 in gingival epithelial cells.…”

Section: Role Of Par-2 In the Induction Of Il-33 By Gingipainsmentioning

confidence: 99%

Possible Roles of IL-33 in Periodontal Diseases: Porphyromonas gingivalis Induced IL-33 in Human Gingival Epithelial Cells

Tada

Shimauchi

Takada

et al. 2015

Interface Oral Health Science 2014

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In the oral mucosa, epithelial cells work not only as a physical barrier to pathogens, but also play a pivotal role in initiating immune responses to microbes. Interleukin (IL)-33, a member of the IL-1 family, is constitutively expressed in epithelial cells and amplifies Th2-type inflammatory immune responses. We found that IL-33 was detected in the inflamed gingival epithelium from chronic periodontitis patients, and periodontopathic Porphyromonas gingivalis strongly increased expressions of IL-33 mRNA and molecules in human gingival epithelial cells. In contrast, fimbriae, a lipopeptide and lipopolysaccharide derived from P. gingivalis were not active in this respect. Protease inhibitors specific for gingipains efficiently inhibited the induction of IL-33 mRNA by stimulation with P. gingivalis. Furthermore, P. gingivalis KDP136, a gingipains-null mutant, did not increase IL-33 mRNA expression. We also demonstrated that P. gingivalis upregulated IL-33 mRNA expression through protease-activated receptor-2, phospholipase C, mitogen-activated protein kinase p38 and NF-κB. IL-33 is suggested to negatively regulate antimicrobial peptide LL-37, resulting in attenuation of innate immune responses of gingival epithelial cells in chronic periodontitis. Possible roles of IL-33 in inflammation in the oral mucosa are discussed.

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Variations of Porphyromonas gingivalis fimbriae in relation to microbial pathogenesis

Abstract: The fimbria variations may have an influence on the development of periodontal disease.

Cited by 213 publications

References 69 publications

Porphyromonas gingivalis Minor Fimbriae Are Required for Cell-Cell Interactions

Porphyromonas gingivalis Minor Fimbriae Are Required for Cell-Cell Interactions

Arginine deiminase inhibits Porphyromonas gingivalis surface attachment

Possible Roles of IL-33 in Periodontal Diseases: Porphyromonas gingivalis Induced IL-33 in Human Gingival Epithelial Cells

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