Abstract
Natural killer cell function is controlled by interaction of NK receptors with MHC I molecules expressed on target cells. We describe the binding of bacterially expressed Ly49A, the prototype murine NK inhibitory receptor, to similarly engineered H-2Dd. Despite its homology to C-type lectins, Ly49A binds independently of carbohydrate and Ca2+ and shows specificity for MHC I but not bound peptide. The affinity of the Ly49A/H-2Dd interaction as determined by surface plasmon resonance is from 6 to 26 microM at 25 degrees C and is greater by ultracentrifugation at 4 degrees C. Biotinylated Ly49A stains H-2Dd-expressing cells. Competition experiments indicate that the Ly49A and T cell receptor (TCR) binding sites on MHC I are distinct, suggesting complex regulation of cells that bear both TCR and NK cell receptors.
MeSH terms
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Animals
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Antigens, Ly*
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Binding Sites
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Binding, Competitive
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Biotinylation
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Calcium / metabolism
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Glycosylation
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H-2 Antigens / metabolism*
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Histocompatibility Antigen H-2D
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Killer Cells, Natural / immunology*
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Lectins, C-Type
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Membrane Glycoproteins / chemistry
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Membrane Glycoproteins / genetics
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Membrane Glycoproteins / metabolism*
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Mice
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Mice, Inbred C57BL
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Models, Molecular
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NK Cell Lectin-Like Receptor Subfamily A
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Peptide Fragments / metabolism
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Protein Binding
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Protein Folding
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Protein Processing, Post-Translational
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Protein Structure, Tertiary
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Receptors, Antigen, T-Cell / metabolism
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Receptors, NK Cell Lectin-Like
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Recombinant Fusion Proteins / metabolism
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Surface Plasmon Resonance
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Ultracentrifugation
Substances
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Antigens, Ly
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H-2 Antigens
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Histocompatibility Antigen H-2D
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Klra1 protein, mouse
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Lectins, C-Type
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Membrane Glycoproteins
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NK Cell Lectin-Like Receptor Subfamily A
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Peptide Fragments
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Receptors, Antigen, T-Cell
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Receptors, NK Cell Lectin-Like
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Recombinant Fusion Proteins
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Calcium