tailieunhanh - Báo cáo y học: "Identification of an altered peptide ligand based on the endogenously presented, rheumatoid arthritis-associated, human cartilage glycoprotein-39(263–275) epitope: an MHC anchor variant peptide for immune modulation"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học General Psychiatry cung cấp cho các bạn kiến thức về ngành y đề tài: Identification of an altered peptide ligand based on the endogenously presented, rheumatoid arthritis-associated, human cartilage glycoprotein-39(263–275) epitope: an MHC anchor variant peptide for immune modulation. | Available online http content 9 4 R71 Research article Identification of an altered peptide ligand based on the endogenously presented rheumatoid arthritis-associated human cartilage glycoprotein-39 263-275 epitope an MHC anchor variant peptide for immune modulation Annemieke MH Boots Henk Hubers Milou Kouwijzer Leontien den Hoed-van Zandbrink Bernice M Westrek-Esselink Cindy van Doorn Rachel Stenger Ebo S Bos Marie-jose C van Lierop Gijs F Verheijden Cornelis M Timmers and Catharina J van Staveren NV Organon Research Laboratories Oss The Netherlands Corresponding author Annemieke MH Boots Received 16 Apr 2007 Revisions requested 13 Jun 2007 Revisions received 25 Jun 2007 Accepted 23 Jul 2007 Published 23 Jul 2007 Arthritis Research Therapy 2007 9 R71 doi ar2269 This article is online at http content 9 4 R71 2007 Boots et al. licensee BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Open Access Abstract We sought to identify an altered peptide ligand APL based on the endogenously expressed synovial auto-epitope of human cartilage glycoprotein-39 HC gp-39 for modulation of cognate HLA-DR4-restricted T cells. For this purpose we employed a panel of well-characterized T cell hybridomas generated from HC gp-39-immunized HLA-DR4 transgenic mice. The hybridomas all respond to the HC gp-39 263-275 epitope when bound to HLA-DR4 B 1 0401 but differ in their fine specificities. First the major histocompatibility complex MHC and T-cell receptor TCR contact residues were identified by analysis of single site substituted analogue peptides for HLA-DR4 binding and cognate T cell recognition using both T hybridomas and polyclonal T cells from peptide-immunized HLA-DR4 .