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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.

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