Abstract
In the last decade, the association between the periodontitis and rheumatoid arthritis (RA) has been established, suggesting that oral microbiome plays a causal role by initiating this chronic autoimmune inflammatory disease of articulation. Both pathogenesis are similar in term of chronic inflammation, tissue breakdown and bone resorption. Molecular aspects have also revealed that citrullination, a post-translational modification catalyzed by peptidyl-arginine deiminases (PADs), is involved in both diseases. For RA, citrullinated proteins production leads to the synthesis the of anti-citrullinated protein antibodies triggering the loss of immune tolerance. In humans, five PADs have been identified. Recently, studies have found that only Porphyromonas species possess PAD. Thus, a major periodontal pathogen, Porphyromonas gingivalis, is able to generate citrullinated epitopes, and could consequently induce anti-citrullinated protein antibodies. In this review, citrullination process, periodontitis and RA are described to put them in relation with molecular, clinical and epidemiological studies establishing the association between periodontitis and RA.
Highlights
SUMMARY Protein arginine deiminase of oral microbiome plays a causal role in the polyarthritis rheumatoid initiating
The association between the periodontitis and rheumatoid arthritis (RA) has been established, suggesting that oral microbiome plays a causal role by initiating this chronic autoimmune inflammatory disease of articulation
Molecular aspects have revealed that citrullination, a posttranslational modification catalyzed by peptidyl-arginine deiminases (PADs), is involved in both diseases
Summary
Ou désimination, est une modification post-traductionnelle des protéines qui consiste en la transformation de résidus peptidyl-arginyl en résidus peptidyl-citrullyl avec libération d’ammonium (Figure 1) [5]. Elle est réalisée par des enzymes appelées peptidylarginine désiminases (PAD, pour protein-arginine deiminase, ou protein-L-arginine iminohydrolase, ou EC 3.5.3.15) (Figure 1) [5]. Ces enzymes n’ont été identifiées que chez Porphyromonas, plus particulièrement chez P. gingivalis, où l’homologue des PAD humaines a été nommé PPAD (P. gingivalis peptidylarginine deiminase) [9]. La PPAD des Porphyromonas présente entre 30 et 40 % d’identité avec les PAD humaines (Tableau I). Contrairement à ses homologues eucaryotes qui sont présentes dans le cytoplasme de la cellule, PPAD est sécrétée ou liée à la membrane externe de la paroi bactérienne. PPAD peut en effet citrulliner des protéines bactériennes et des protéines de l’hôte, alors que les PAD n’agissent que sur des protéines humaines
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