The HLA–B*2705 peptidome
✍ Scribed by Lilach Ben Dror; Eilon Barnea; Ilan Beer; Matthias Mann; Arie Admon
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- English
- Weight
- 149 KB
- Volume
- 62
- Category
- Article
- ISSN
- 0004-3591
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📜 SIMILAR VOLUMES
High-affinity ligands of non-peptidic nature, binding to the class I major histocompatibility complex protein HLA B\*2705 whose expression is strongly linked to the pathogenesis of the autoimmune disease ankylosing spondylitis, should give way to a selective immunotherapy by blocking or antagonising
Eight nonamer peptides that comply with the major anchor residue motifs (the combination of amino acid residues at positions 2 and 9), R - K and R - R, of HLA-B27 (B\*2705)-binding peptides were synthesized and tested for their direct binding to HLA class I alpha chains by the HLA class I alpha chai
Objective. The association of reactive arthritis (ReA) with HLA-B27 and the presence of bacterial antigen in joints with ReA suggest that bacterial peptides might be presented by the HLA-B27 molecule and thus stimulate CD8 T cells. This study was performed to investigate the B27-restricted cytotoxic