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Minor histocompatibility Ags elicit cell-mediated immune responses and graft rejection in individuals receiving MHC-matched tissues. H60 represents a dominant Ag that elicits a strong CTL response in C57BL/6 mice immunized against BALB.B. An 8-aa peptide in the H60 protein is presented by H-2K(b) and this is recognized by the TCR as an alloantigen. The intact H60 glycoprotein is a ligand for the costimulatory NKG2D receptor that is expressed by activated CD8(+) T cells. Thus, H60 may provide both an allogeneic peptide and its own costimulation. We show that mutation of an H-2K(b)-binding anchor residue in the H60 peptide completely abrogates binding of H60 glycoprotein to NKG2D and a synthetic H60 peptide partially blocks the binding of NKG2D to its ligand. Ligands of the human NKG2D receptor are remarkably polymorphic, suggesting that these may also serve as minor histocompatibility Ags.

Type

Journal article

Journal

J Immunol

Publication Date

01/04/2002

Volume

168

Pages

3131 - 3134

Keywords

Animals, Antigen Presentation, Binding, Competitive, Cell Line, Cytotoxicity Tests, Immunologic, Cytotoxicity, Immunologic, H-2 Antigens, Immunodominant Epitopes, Killer Cells, Natural, Mice, Mice, Inbred BALB C, Mice, Inbred C57BL, Minor Histocompatibility Antigens, Mutagenesis, Site-Directed, NK Cell Lectin-Like Receptor Subfamily K, Oligopeptides, Protein Binding, Receptors, Antigen, T-Cell, Receptors, Immunologic, Receptors, Natural Killer Cell, Solubility