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Cytotoxic T cells (CTL) recognize short peptide epitopes presented by class I glycoproteins encoded by the major histocompatibility complex (MHC). It is not yet known whether peptides containing posttranslationally modified amino acids can also be recognized by CTL. To address this issue, we have studied the immunogenicity and recognition of a glycopeptide carrying an O-linked N-acetylglucosamine (GlcNAc) monosaccharide-substituted serine residue. This posttranslational modification is catalyzed by a recently described cytosolic glycosyltransferase. We show that glycosylation does not affect peptide binding to MHC class I and that glycopeptides can elicit a strong CTL response that is glycopeptide specific. Furthermore, glycopeptide recognition by cytotoxic T cells is dependent on the chemical structure of the glycan as well as its position within the peptide.

Original publication

DOI

10.1084/jem.180.2.739

Type

Journal article

Journal

J Exp Med

Publication Date

01/08/1994

Volume

180

Pages

739 - 744

Keywords

Amino Acid Sequence, Carbohydrates, Cell Line, Glycoproteins, Histocompatibility Antigens Class I, Molecular Sequence Data, Protein Processing, Post-Translational, T-Lymphocytes, Cytotoxic