Identification of the minimal glycopeptide core recognized by T cells in a model for rheumatoid arthritis
| Autor: | Peter Kjellén, Jan Kihlberg, Lotta Holm, Rikard Holmdahl |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
musculoskeletal diseases
animal structures Glycosylation T-Lymphocytes Molecular Sequence Data Clinical Biochemistry Type II collagen Pharmaceutical Science Peptide macromolecular substances Biochemistry Epitope Cell Line Epitopes Mice Structure-Activity Relationship chemistry.chemical_compound Drug Discovery Animals Amino Acid Sequence Binding site Collagen Type II Molecular Biology Peptide sequence chemistry.chemical_classification Binding Sites Hybridomas Organic Chemistry Glycopeptides Histocompatibility Antigens Class II Arthritis Experimental Molecular biology Peptide Fragments Glycopeptide Hydroxylysine chemistry Immunology Molecular Medicine |
| Zdroj: | Bioorganic & Medicinal Chemistry. 13:473-482 |
| ISSN: | 0968-0896 |
| DOI: | 10.1016/j.bmc.2004.10.011 |
| Popis: | 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 A(q), a MHC-II molecule associated with development of CIA. Binding to A(q) correlated well with predictions from a computer-based model. T-cell hybridomas, obtained in CIA, were also used to study the ability of A(q) 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 beta-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. |
| Databáze: | OpenAIRE |
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