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The collagen type II (CII) 263–272 peptide is a predominant T and B cell antigenic peptide in rheumatoid arthritis.1 Crystallographic data showed that 263F and 264K of CII263–272 are mainly responsible for binding with HLA-DR, and that 267Q and 270K were the major T cell receptor (TCR)-contact residues.2,3 We have shown that the CII altered peptide ligand (APL) with individual or consecutive substitutions of the TCR-contact amino acids could inhibit T cell activation induced by wild-type CII peptide in the context of HLA-DRB1, among which the most potent T cell activation suppressor is sub268–270, in which the amino acids of wild-type CII263–272 at positions 268, 269 and 270 were substituted with glycine or alanine (FKGEQAGAGE, substitutions underlined).4,5 Collagen-induced arthritis (CIA) is induced by wild-type CII in susceptible rodent strains. …
Funding: This work was supported by a grant from the National Science Foundation of China (30271223) and the Key Project grant of Beijing Municipal Science Foundation (7041005).
Competing interests: None.