Isabelle Auger INSERM Researcher
Course and current status
Name: Isabelle AUGER
Adress: INSERM UMRs1097, Parc Scientifique de Luminy, case 939, 163 Avenue de Luminy, 13288 Marseille cedex 09, France. Tel: + 33 4 91 82 87 50. Fax: + 33 4 91 83 09 26. Email: isabelle.auger@inserm.fr
Personal: Date of birth: August, 20, 1970. Place of birth: Marseille, France. Citizenship: French. Languages: French, English.
Current position: INSERM Researcher, INSERM UMRs1097, Immunogenetics of rheumatoid arthritis, Marseille, France.
Education: Luminy Science University, Marseille, France, (PhD, 1997).
Qualifications: HDR, 2005 (Immunology, University Medical School, Marseille, France). PhD, 1997 (Immunology, Luminy Science University, Marseille, France).
Research Experience: Post doctoral position, INSERM U463, Institut de Biologie, Nantes, France (1998-1999). Post doctoral position, INSERM U639, Marseille, France (1997-1998).
Patent applications:
- 2019: PCT/EP2020/056015: New vaccinal strategy to prevent or treat rheumatoid arthritis.
- 2013-2015: Licence BIORAD 121024A30.
- 2012: EP11028: Method diagnostic of Scleroderma.
- 2011: WO2012156313, EP11305584.2: Method for the diagnosis of early rheumatoid arthritis.
- 2010: WO2010115745A3: Biomarkers, Methods and kits for diagnosis of rheumatoid arthritis.
- 2009: WO2009138408B, EP08305167.2: Methods and kits for the diagnosis of rheumatoid arthritis.
Scientific summary
Rheumatoid arthritis (RA) is a chronic inflammatory joint disease causing articular cartilage and bone destruction. Its worldwide prevalence is 1%, its cause is unknown.
RA is an autoantibody mediated disease. Among the various autoantibodies known in RA, autoantibodies to citrullinated proteins (ACPAs) are highly specific. Citrulline is generated by post translational conversion of arginine residues. This process is catalyzed by a group of enzymes called calcium dependent peptidyl arginine deiminases, PAD. ACPAs recognize citrulline on different proteins like filaggrin, vimentin or fibrin. The mechanisms leading to the production of ACPAs are unknown. We propose a model to explain the emergence of anti-citrullinated protein autoantibodies in RA: immunization to PAD proteins triggers ACPAs through a hapten/carrier mechanism in which the carrier is PAD, which performs citrullination, and the hapten is any protein being citrullinated by PAD.
Our results allow us to understand the birth of anti-citrullin autoimmunity: indeed, if T cell recognition of PAD helps the development of ACPAs, then, tolerization to PAD might allow to prevent the production of ACPAs and maybe of rheumatoid arthritis.
