Cutting Edge: The Conversion of Arginine to Citrulline Allows for a High-Affinity Peptide Interaction with the Rheumatoid Arthritis-Associated HLA-DRB1*0401 MHC Class II Molecule1

By J. Hill, S. Southwood, Alessandro Sette, A. Jevnikar, D. Bell, E. Cairns. Journal of Immunology, 2003

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A new model for an etiology of rheumatoid arthritis: smoking may trigger HLA-DR (shared epitope)-restricted immune reactions to autoantigens modified by citrullination. (2006, background): “An immune response to the citrullinated proteins might then be preferentially induced in individuals carrying the HLA–DR SE genes, since citrullination has been demonstrated to increase the binding of modified peptides to SE-containing HLA–DR antigens and thereby to enhance the immunogenicity of the”
Immunopathogenesis of rheumatoid arthritis (2017, neutral): “For example, citrullinated vimentin peptides bind much more avidly to the RA HLA-DR than does native protein; in contrast, other MHCs do not exhibit this differential binding (Hill et al., 2003; Law et al., 2012).”