Recognition of carbohydrate by major histocompatibility complex class I-restricted, glycopeptide-specific cytotoxic T lymphocytes.

作者：John Sørensen Haurum, Gemma Arsequell, Annemarie Coffman Lellouch, Siew Yee Wong, Raymond Allen Dwek, Andrew James McMichael, Tim J Elliott · 发表于：The Journal of Experimental Medicine · 年份：1994 · DOI：10.1084/jem.180.2.739 · 被引用次数：184 · 研究领域：Glycosylation and Glycoproteins Research、Immune Cell Function and Interaction、Galectins and Cancer Biology

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.