{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,17]],"date-time":"2025-10-17T13:29:58Z","timestamp":1760707798892},"reference-count":44,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2005,11,23]],"date-time":"2005-11-23T00:00:00Z","timestamp":1132704000000},"content-version":"vor","delay-in-days":5075,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Eur J Immunol"],"published-print":{"date-parts":[[1992,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>CD4<jats:sup>+<\/jats:sup> T cells recognize antigenic peptides bound to the polymorphic peptide\u2010binding site of major histocompatibility complex (MHC) class II molecules. The polymorphism of this site is thought to dictate which peptides can be bound and thus presented to the T cell receptor. The mycobacterial 65\u2010kDa heat\u2010shock protein (hsp65) peptide 3\u201013 is an important T cell epitope: it is immunodominant in the mycobacterium\u2010specific T cell response of HLA\u2010DR3<jats:sup>+<\/jats:sup> individuals but, interestingly cannot be recognized in the context of any other HLA\u2010DR molecules. We, therefore, have tested whether the hsp65 epitope p3\u201013 is selected for T cell recognition in the context of only HLA\u2010DR3 molecules by an unique binding specificity for HLA\u2010DR3. Using biotinylated peptides and EBV\u2010transformed BLCL comprising all known HLA class II specificities, we find that p3\u201013 binds to HLA\u2010DRw17(DR3) but not to any other HLA\u2010DR molecule. Conversely, a control peptide p307\u2010319 influenza hemagglutinin binds to all known HLA\u2010DR molecules but only weakly to HLA\u2010DRw17 and HLA\u2010DR9. Peptide binding could be inhibited by excess unbiotinylated competitor analogue as well as by anti\u2010DR monoclonal antibodies but not by anti\u2010class I\u2010, anti\u2010DP\u2010 or anti\u2010DQ monoclonal antibodies.<\/jats:p><jats:p>The amino acid sequence of DRw17 molecules differs uniquely at five positions from the other DR\u03b21 sequences. Three of these five residues (positions 26, 71 and 74) are potential peptide contacting residues. These residues map closely together in the hypothetical three\u2010dimensional model of the DR molecule and, thus, most probably form a positively charged pocket, critical for the binding of p3\u201013. Interestingly, p3\u201013 does not bind to a DR3 variant, the DRw18 molecule. The DRw18\u03b21 chain differs from DRw17 at two major positions, close to or within the DRw17\u2010specific pocket. These substitutions drastically change the structure and charge of the pocket and thus presumably abrogate its ability to bind p3\u201013.<\/jats:p>","DOI":"10.1002\/eji.1830220117","type":"journal-article","created":{"date-parts":[[2007,3,1]],"date-time":"2007-03-01T13:01:26Z","timestamp":1172754086000},"page":"107-113","source":"Crossref","is-referenced-by-count":41,"title":["Binding of a major T cell epitope of mycobacteria to a specific pocket within HLA\u2010DRw17(DR3) molecules"],"prefix":"10.1002","volume":"22","author":[{"given":"Annemieke","family":"Geluk","sequence":"first","affiliation":[]},{"given":"Wim","family":"Bloemhoff","sequence":"additional","affiliation":[]},{"given":"Ren\u00e9 R. P.","family":"De Vries","sequence":"additional","affiliation":[]},{"given":"Tom H. 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