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Two synthetic O-GlcNAc-bearing peptides that elicit H-2Db-restricted glycopeptide-specific cytotoxic T cells (CTL) have been shown to display nonreciprocal patterns of cross-reactivity. Here, we present the crystal structures of the H-2Db glycopeptide complexes to 2.85 A resolution or better. In both cases, the glycan is solvent exposed and available for direct recognition by the T cell receptor (TCR). We have modeled the complex formed between the MHC-glycopeptide complexes and their respective TCRs, showing that a single saccharide residue can be accommodated in the standard TCR-MHC geometry. The models also reveal a possible molecular basis for the observed cross-reactivity patterns of the CTL clones, which appear to be influenced by the length of the CDR3 loop and the nature of the immunizing ligand.

Original publication

DOI

10.1016/s1074-7613(00)80007-2

Type

Journal article

Journal

Immunity

Publication Date

01/1999

Volume

10

Pages

63 - 74

Keywords

Acetylglucosamine, Animals, Clone Cells, Crystallography, X-Ray, Cytotoxicity, Immunologic, Epitopes, T-Lymphocyte, Glycopeptides, H-2 Antigens, Histocompatibility Antigen H-2D, Humans, Macromolecular Substances, Mice, Models, Molecular, Nucleocapsid Proteins, Nucleoproteins, Oligopeptides, Polysaccharides, Receptors, Antigen, T-Cell, T-Lymphocytes, Cytotoxic, Viral Core Proteins