{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,25]],"date-time":"2025-10-25T18:54:00Z","timestamp":1761418440804},"reference-count":52,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2005,12,6]],"date-time":"2005-12-06T00:00:00Z","timestamp":1133827200000},"content-version":"vor","delay-in-days":3202,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Eur J Immunol"],"published-print":{"date-parts":[[1997,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Previous studies have shown that the presentation of some bacterial superantigens by major histocompatibility complex (MHC) class II molecules is strongly influenced by class II\u2010associated peptides. For example, presentation of the toxic shock syndrome toxin\u20101 (TSST\u20101) superantigen by antigen\u2010processing\u2010defective T2\u2010I\u2010A<jats:sup>b<\/jats:sup> cells (which expresses I\u2010A<jats:sup>b<\/jats:sup> that is either empty or associated with invariant chain\u2010derived peptides) can be strongly enhanced by some, but not other, I\u2010A<jats:sup>b<\/jats:sup>\u2010binding peptides. Here we investigate the contribution of I\u2010A<jats:sup>b<\/jats:sup>\u2010associated peptides in the presentation of TSST\u20101 to T cells. The data show that overlapping peptides expressing the same core I\u2010A<jats:sup>b<\/jats:sup>\u2010restricted epitope, but with various N and C termini, can differ profoundly in their ability to promote TSST\u20101 presentation to T cells. Analysis of altered and truncated peptides indicates that residues at the C\u2010terminal end of the peptide have a dramatic effect on TSST\u20101 presentation. This effect does not involve a cognate interaction between the peptide and the TSST\u20101 molecule, but appears to depend on the length of the C\u2010terminal region. These data are consistent with crystallographic studies suggesting that TSST\u20101 may interact with the C\u2010terminal residues of MHC class II\u2010associated peptides. We also examined the capacity of naturally processed peptides to promote TSST\u20101 binding using a superantigen blocking assay. The data demonstrated that a naturally processed epitope is dominated by peptides that do not promote strong TSST\u20101 binding to I\u2010A<jats:sup>b<\/jats:sup>. Taken together, these data suggest that TSST\u20101 binding to MHC class II molecules is controlled by the C\u2010terminal residues of the associated peptide, and that many naturally processed peptide\/class II complexes do not present TSST\u20101 to T cells. Thus, the peptide dependence of TSST\u20101 binding to class II molecules may significantly reduce the capacity of TSST\u20101 to stimulate T cells.<\/jats:p>","DOI":"10.1002\/eji.1830270328","type":"journal-article","created":{"date-parts":[[2007,3,2]],"date-time":"2007-03-02T04:32:52Z","timestamp":1172809972000},"page":"772-781","source":"Crossref","is-referenced-by-count":19,"title":["Carboxy\u2010terminal residues of major histocompatibility complex class II\u2010associated peptides control the presentation of the bacterial superantigen toxic shock syndrome toxin\u20101 to T cells"],"prefix":"10.1002","volume":"27","author":[{"given":"Renren","family":"Wen","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dana R.","family":"Broussard","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sherri","family":"Surman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Twala L.","family":"Hogg","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marcia A.","family":"Blackman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David L.","family":"Woodland","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2005,12,6]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0065-2776(08)60534-9"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.2185544"},{"key":"e_1_2_1_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0065-2776(08)60821-4"},{"key":"e_1_2_1_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(90)90388-U"},{"key":"e_1_2_1_6_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.91.18.8462"},{"key":"e_1_2_1_7_2","doi-asserted-by":"publisher","DOI":"10.1038\/369324a0"},{"key":"e_1_2_1_8_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.88.2.613"},{"key":"e_1_2_1_9_2","doi-asserted-by":"publisher","DOI":"10.1038\/339221a0"},{"key":"e_1_2_1_10_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.2658055"},{"key":"e_1_2_1_11_2","doi-asserted-by":"publisher","DOI":"10.1016\/0008-8749(92)90147-H"},{"key":"e_1_2_1_12_2","doi-asserted-by":"crossref","first-page":"463","DOI":"10.4049\/jimmunol.146.2.463","volume":"146","author":"Mollick J. 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