Advanced search
Start date

Porphyromonas gingivalis peptidylarginine deiminase (PPAD): biochemical evaluation of a novel link for breaching immunologic tolerance in rheumatoid arthritis

Grant number: 23/03753-1
Support Opportunities:Scholarships abroad - Research Internship - Doctorate (Direct)
Effective date (Start): April 01, 2024
Effective date (End): March 31, 2025
Field of knowledge:Health Sciences - Dentistry - Periodontology
Principal Investigator:Mario Taba Junior
Grantee:Ana Carolina Aparecida Rivas
Supervisor: Felipe Andrade
Host Institution: Faculdade de Odontologia de Ribeirão Preto (FORP). Universidade de São Paulo (USP). Ribeirão Preto , SP, Brazil
Research place: Johns Hopkins University (JHU), United States  
Associated to the scholarship:21/02523-7 - Evaluation of the effects of specific inhibition of IL6R on ligature-induced Periodontitis in rats with experimental Rheumatoid Arthritis, BP.DD


Porphyromonas gingivalis peptidylarginine deiminase (PPAD) is a bacterial deiminase unrelated evolutionarily to human PAD and has been of considerable importance in unraveling a mechanism linking periodontal disease (PD), onset of rheumatoid arthritis, and bacterial citrullination. PD, which leads to an increase in the number of P. gingivalis, is a chronic inflammatory disease caused by infection of the supporting tissues of the teeth, affecting alveolar bone and causing tooth loss. It has been reported that patients with RA have a higher prevalence of PD and that peptidylarginine deiminase (PPAD) from Porphyromonas gingivalis generated by P. gingivalis infection in periodontal disease has been implicated in the onset of RA by generating citrullinated neoantigens.Studies suggest that Porphyromonas gingivalis may be involved in lead off auto-reactive immune responses and triggering immune diseases such as RA. Therefore, the aim of this study is to investigate the Porphyromonas gingivalis peptidylarginine deiminase (PPAD) from P.g. CH2007 (RACH2007-PPAD) in serum samples from patients with rheumatoid arthritis (RA) and a PPAD citrullinated peptide (CPP) containing the major site of autocitrullination as potential targets for antibody reactivity in RA and to analyze the possibility of native human citrullinating proteins by PPAD in the context of RA.Key words: Porphyromona gingivalis, bacterial microbiology, periodontal disease, rheumatoid arthritis, host. (AU)

News published in Agência FAPESP Newsletter about the scholarship:
Articles published in other media outlets (0 total):
More itemsLess items

Please report errors in scientific publications list using this form.