Myelin basic protein peptide complexes with the class II MHC molecules I-Au and I-Ak form and dissociate rapidly at neutral pH
| Autor: | K Mason, D W Denney, H M McConnell |
|---|---|
| Rok vydání: | 1995 |
| Předmět: | |
| Zdroj: | The Journal of Immunology. 154:5216-5227 |
| ISSN: | 1550-6606 0022-1767 |
| DOI: | 10.4049/jimmunol.154.10.5216 |
| Popis: | The acetylated N-terminal peptide of myelin basic protein (MBP) is the immunodominant T cell epitope in the induction of experimental autoimmune encephalomyelitis in the I-Au- and I-Ak-expressing mouse strains. We used a direct binding assay to examine the kinetics of binding and dissociation of a series of MBP peptide analogues with the affinity-purified class II MHC molecules I-Au and I-Ak. We observe much faster in vitro rates of binding and dissociation than has been reported previously for other immunogenic peptides at neutral pH. The kinetics also reveal inactivation of the peptide-free class II MHC molecules. These results are consistent with previously proposed mechanisms for tolerance escape and autoimmune disease. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|