{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,21]],"date-time":"2026-08-21T12:58:26Z","timestamp":1787317106521,"version":"build-2736575974"},"reference-count":28,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2005,1,28]],"date-time":"2005-01-28T00:00:00Z","timestamp":1106870400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Eur J Immunol"],"published-print":{"date-parts":[[2005,2]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Type II collagen (CII) is a target for autoreactive T cells in both rheumatoid arthritis and the murine model collagen\u2010induced arthritis. The determinant core of CII has been identified as CII260\u2013270, and the alteration of this T cell epitope by posttranslational modifications is known to be critical for development of arthritis in mice. Using CII\u2010specific T cell hybridomas we have now shown that the immunodominant T cell epitope in the normal (healthy) human and rat joint cartilage is O\u2010glycosylated at the critical T cell receptor recognition position 264 with a mono\u2010 or di\u2010saccharide attached to a hydroxylysine. In contrast, in the arthritic human and rat joint cartilage there are both glycosylated and non\u2010glycosylated CII forms. Glycosylated CII from normal cartilage could not be recognized by T cells reactive to peptides having only lysine or hydroxylysine at position 264, showing that antigen\u2010presenting cells could not degrade the O\u2010linked carbohydrate. Thus, the variable forms of the glycosylated epitope are determined by the structures present in cartilage, and these vary during the disease course. We conclude that the chondrocyte determines the structures presented to the immune system and that these structures are different in normal versus arthritic states.<\/jats:p>\n                  <jats:p>\n                    See accompanying Commentary:\n                    <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"doi\" xlink:href=\"10.1002\/eji.200425889\">http:\/\/dx.doi.org\/10.1002\/eji.200425889<\/jats:ext-link>\n                  <\/jats:p>","DOI":"10.1002\/eji.200425637","type":"journal-article","created":{"date-parts":[[2005,1,28]],"date-time":"2005-01-28T08:18:23Z","timestamp":1106900303000},"page":"357-366","source":"Crossref","is-referenced-by-count":68,"title":["The major T cell epitope on type II collagen is glycosylated in normal cartilage but modified by arthritis in both rats and humans"],"prefix":"10.1002","volume":"35","author":[{"given":"Balik","family":"Dzhambazov","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Meirav","family":"Holmdahl","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hisakata","family":"Yamada","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shemin","family":"Lu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mikael","family":"Vestberg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bj\u00f6rn","family":"Holm","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olof","family":"Johnell","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jan","family":"Kihlberg","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rikard","family":"Holmdahl","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2005,1,28]]},"reference":[{"key":"e_1_2_7_1_2","doi-asserted-by":"publisher","DOI":"10.1002\/1529-0131(199910)42:10<2085::AID-ANR8>3.0.CO;2-Z"},{"key":"e_1_2_7_2_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.86.2.636"},{"key":"e_1_2_7_3_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.132254199"},{"key":"e_1_2_7_4_2","doi-asserted-by":"publisher","DOI":"10.1056\/NEJM197804202981602"},{"key":"e_1_2_7_5_2","doi-asserted-by":"publisher","DOI":"10.1002\/art.1780301102"},{"key":"e_1_2_7_6_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.154.3.688"},{"key":"e_1_2_7_7_2","doi-asserted-by":"publisher","DOI":"10.1002\/eji.1830240736"},{"key":"e_1_2_7_8_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.185.6.1113"},{"key":"e_1_2_7_9_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.95.13.7574"},{"key":"e_1_2_7_10_2","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1521-4141(199802)28:02<755::AID-IMMU755>3.0.CO;2-2"},{"key":"e_1_2_7_11_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.180.2.745"},{"key":"e_1_2_7_12_2","doi-asserted-by":"publisher","DOI":"10.1002\/eji.1830260835"},{"key":"e_1_2_7_13_2","doi-asserted-by":"publisher","DOI":"10.1002\/(SICI)1521-4141(199808)28:08<2580::AID-IMMU2580>3.0.CO;2-X"},{"key":"e_1_2_7_14_2","first-page":"53","article-title":"The hydroxylation of prolyl and lysyl residues.","author":"Kivirikko K. 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