Identification of the minimal glycopeptide core recognized by T cells in a model for rheumatoid arthritis Original Research Article

Collagen induced arthritis (CIA) is a common mouse model for rheumatoid arthritis. Two sets of truncated peptides derived from type II collagen have been prepared and tested for binding to Aq, a MHC-II molecule associated with development of CIA. Binding to Aq correlated well with predictions from a computer-based model. T-cell hybridomas, obtained in CIA, were also used to study the ability of Aq bound peptides to trigger a T-cell response. The minimal peptide epitope required for binding, as well as for giving a T-cell response, was determined to be CII260–267. In collagen this epitope is often glycosylated at hydroxylysine 264 and glycosylation has been shown to be an immunodominant feature in CIA. Synthesis and evaluation of CII260–267 carrying a β-d-galactosyl moiety at position 264 revealed that this glycopeptide stimulated representative members from a panel of carbohydrate-specific T-cell hybridomas obtained in CIA.