Key Points Clonal-like expansion of NK cells in response to CMV infection causes stable imprints in the human KIR repertoire. Education by inhibitory KIRs promotes the expansion of NK cells, causing repertoire skewing and a bias for self-specific inhibitory KIRs.

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Human NK cells and subsets of T cells or NKT cells express the orphan C-type lectin receptor CD161 (NKR-P1A) of unknown function. In contrast to rodents that possess several NKR-P1 genes coding for either activating or inhibitory receptors, the nature of signals delivered by the single human NKR-P1A receptor is still to be clarified. In this article, we show that the lectin-like transcript 1 (LLT1) molecule is a ligand for the CD161 receptor. Engagement of CD161 on NK cells with LLT1 expressed on target cells inhibited NK cell-mediated cytotoxicity and IFN-γ secretion. Conversely, LLT1/CD161 interaction in the presence of a TCR signal enhanced IFN-γ production by T cells. These findings identify a novel ligand/receptor pair that differentially regulate NK and T cell functions.

Objective. HLA-B27 is capable of forming in vitro a heavy-chain homodimer structure lacking ␤ 2 -microglobulin. We undertook this study to ascertain if patients with spondylarthritis express ␤ 2 -microglobulinfree HLA-B27 heavy chains in the form of homodimers and receptors for HLA-B27 homodimers.Methods. Expression of HLA-B27 heavy chains by mononuclear cells was analyzed by fluorescenceactivated cell sorter staining, Western blotting with the monoclonal antibody HC-10, and 2-dimensional isoelectric focusing. Fluorescence-labeled tetrameric complexes of HLA-B27 heavy-chain homodimers were constructed in which each dimer comprised one His-tagged heavy chain and one biotinylated heavy chain, and were used to stain patient and control mononuclear cells and transfected cell lines.Results. Patients with spondylarthritis expressed cell-surface HLA-B27 homodimers. Populations of synovial and peripheral blood monocytes, and B and T lymphocytes from patients with spondylarthritis, and controls carried receptors for HLA-B27 homodimers.