| First Author | Bäcklund J | Year | 2002 |
| Journal | Eur J Immunol | Volume | 32 |
| Issue | 12 | Pages | 3776-84 |
| PubMed ID | 12516572 | Mgi Jnum | J:129160 |
| Mgi Id | MGI:3768752 | Doi | 10.1002/1521-4141(200212)32:12<3776::AID-IMMU3776>3.0.CO;2-A |
| Citation | Backlund J, et al. (2002) Glycosylation of type II collagen is of major importance for T cell tolerance and pathology in collagen-induced arthritis. Eur J Immunol 32(12):3776-84 |
| abstractText | Type II collagen (CII) is a candidate cartilage-specific autoantigen, which can become post-translationally modified by hydroxylation and glycosylation. T cell recognition of CII is essential for the development of murine collagen-induced arthritis (CIA) and also occurs in rheumatoid arthritis (RA). The common denominator of murine CIA and human RA is the presentation of an immunodominant CII-derived glycosylated peptide on murine Aq and human DR4 molecules, respectively. To investigate the importance of T cell recognition of glycosylated CII in CIA development after immunization with heterologous CII, we treated neonatal mice with different heterologous CII-peptides (non-modified, hydroxylated and galactosylated). Treatment with the galactosylated peptide (galactose at position 264) was superior in protecting mice from CIA. Protection was accompanied by a reduced antibody response to CII and by an impaired T cell response to the glycopeptide. To investigate the importance of glycopeptide recognition in an autologous CIA model, we treated MMC-transgenic mice, which express the heterologous CII epitope with a glutamic acid in position 266 in cartilage, with CII-peptides. Again, a strong vaccination potential of the glycopeptide was seen. Hence CII-glycopeptides may be the optimal choice of vaccination target in RA, since humans share the same epitope as the MMC mouse. |
