Bacterial and human peptidylarginine deiminases: targets for inhibiting the autoimmune response in rheumatoid arthritis?

Arthritis Res Ther. 2010;12(3):209. doi: 10.1186/ar3000. Epub 2010 Jun 2.


Peptidylarginine deiminases (PADs) convert arginine within a peptide (peptidylarginine) into peptidylcitrulline. Citrullination by human PADs is important in normal physiology and inflammation. Porphyromonas gingivalis, a major pathogen in periodontitis, is the only prokaryote described to possess PAD. P. gingivalis infection may generate citrullinated peptides, which trigger anti-citrullinated peptide antibodies. In susceptible individuals, host protein citrullination by human PADs in the joint probably perpetuates antibody formation, paving the way for the development of chronic arthritis. Blockades of bacterial and human PADs may act as powerful novel therapies by inhibiting the generation of the antigens that trigger and sustain autoimmunity in rheumatoid arthritis.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arthritis, Rheumatoid / epidemiology
  • Arthritis, Rheumatoid / physiopathology*
  • Autoimmunity / physiology*
  • Humans
  • Hydrolases / physiology*
  • Molecular Sequence Data
  • Periodontitis / complications
  • Porphyromonas gingivalis / physiology
  • Protein-Arginine Deiminases
  • Risk Factors


  • Hydrolases
  • Protein-Arginine Deiminases