{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,10]],"date-time":"2026-02-10T11:07:34Z","timestamp":1770721654696,"version":"3.49.0"},"reference-count":34,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2005,11,23]],"date-time":"2005-11-23T00:00:00Z","timestamp":1132704000000},"content-version":"vor","delay-in-days":3645,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Eur J Immunol"],"published-print":{"date-parts":[[1995,12]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>This study extends our previous observation that glycopeptides bind to class I major histocompatibility complex (MHC) molecules and elicit carbohydrate\u2010specific CTL responses. The Sendai virus nucleoprotein wild\u2010type (WT) peptide (FAPGNYPAL) binds H\u20102D<jats:sup>b<\/jats:sup> using the P5\u2010Asn as an anchor. The peptide K2 carrying a P5 serine substitution did not bind D<jats:sup>b<\/jats:sup>. Surprisingly, glycosylation of the serine (K2\u2010O\u2010GlcNAc) with N\u2010acetylglucosamine (GlcNAc), a novel cytosolic O\u2010linked glycosylation, partially restored peptide binding to D<jats:sup>b<\/jats:sup>. We argue that the N\u2010acetyl group of GlcNAc may fulfil the hydrogen bonding requirements of the D<jats:sup>b<\/jats:sup> pocket which normally accomodates P5\u2010Asn. Glycosylation of the P5\u2010Asn residue itself abrogated binding similar to K2, probably for steric reasons. The peptide K2\u2010O\u2010GlcNAc readily elicited D<jats:sup>b<\/jats:sup>\u2010restricted cytotoxic T lymphocytes (CTL), which did not cross\u2010react with K2 or WT. However, all D<jats:sup>b<\/jats:sup>\u2010restricted CTL raised against K2\u2010O\u2010GlcNAc cross\u2010reacted strongly with another glycopeptide, K3\u2010O\u2010GlcNAc, where the GlcNAc substitution is on a neighboring P4\u2010Ser. Furthermore, D<jats:sup>b<\/jats:sup>\u2010restricted CTL clones raised against K2\u2010O\u2010GlcNAc or K3\u2010O\u2010GlcNAc displayed a striking TCR conservation. Our interpretation is that the carbohydrate of K2\u2010O\u2010GlcNAc not only mediates binding to D<jats:sup>b<\/jats:sup>, but also interacts with the TCR in such a way as to mimic K3\u2010O\u2010GlcNAc. This unusual example of molecular mimicry extends the known effects of peptide glycosylation from what we and others have previously reported: glycosylation may create a T cell neo\u2010epitope, or, conversely, abrogate recognition. Alternatively, glycosylation may block peptide binding to MHC class I and finally, as reported here, restore binding, presumably through direct interaction of the carbohydrate with the MHC molecule.<\/jats:p>","DOI":"10.1002\/eji.1830251211","type":"journal-article","created":{"date-parts":[[2007,3,1]],"date-time":"2007-03-01T23:36:53Z","timestamp":1172792213000},"page":"3270-3276","source":"Crossref","is-referenced-by-count":62,"title":["Peptide anchor residue glycosylation: effect on class I major histocompatibility complex binding and cytotoxic T lymphocyte recognition"],"prefix":"10.1002","volume":"25","author":[{"given":"John S.","family":"Haurum","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Linda","family":"Tan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gemma","family":"Arsequell","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Penny","family":"Frodsham","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Annemarie C.","family":"Lellouch","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Paul A. 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