Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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.

Original publication




Journal article


J Immunol

Publication Date





3131 - 3134


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