The peptidylarginine deiminase gene is a conserved feature of Porphyromonas gingivalis

Giorgio Gabarrini, Menke de Smit, Johanna Westra, Elisabeth Brouwer, Arjan Vissink, Kai Zhou, John W. A. Rossen, Tim Stobernack, Jan Maarten van Dijl, Arie Jan van Winkelhoff*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

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Abstract

Periodontitis is an infective process that ultimately leads to destruction of the soft and hard tissues that support the teeth (the periodontium). Periodontitis has been proposed as a candidate risk factor for development of the autoimmune disease rheumatoid arthritis (RA). Porphyromonas gingivalis, a major periodontal pathogen, is the only known prokaryote expressing a peptidyl arginine deiminase (PAD) enzyme necessary for protein citrullination. Antibodies to citrullinated proteins (anti-citrullinated protein antibodies, ACPA) are highly specific for RA and precede disease onset. Objective of this study was to assess P. gingivalis PAD (PPAD) gene expression and citrullination patterns in representative samples of P. gingivalis clinical isolates derived from periodontitis patients with and without RA and in related microbes of the Porphyromonas genus. Our findings indicate that PPAD is omnipresent in P. gingivalis, but absent in related species. No significant differences were found in the composition and expression of the PPAD gene of P. gingivalis regardless of the presence of RA or periodontal disease phenotypes. From this study it can be concluded that if P. gingivalis plays a role in RA, it is unlikely to originate from a variation in PPAD gene expression.

Original languageEnglish
Article number13936
Number of pages8
JournalScientific Reports
Volume5
DOIs
Publication statusPublished - 25-Sep-2015

Keywords

  • RHEUMATOID-ARTHRITIS
  • PERIODONTITIS
  • PURIFICATION
  • ANTIBODIES
  • FIBRINOGEN
  • ENOLASE

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