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The Journal of Immunology, 2000, 165: 6922-6932.
Copyright © 2000 by The American Association of Immunologists

Mapping the Ligand of the NK Inhibitory Receptor Ly49A on Living Cells

Doo Hyun Chung*, Kannan Natarajan*, Lisa F. Boyd*, José Tormo{dagger}, Roy A. Mariuzza{ddagger}, Wayne M. Yokoyama§ and David H. Margulies1,*

* Molecular Biology Section, Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892; {dagger} Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Cientificas, Campus de la Universidad Autónoma de Madrid, Madrid, Spain; {ddagger} Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, MD 20850; and § Division of Rheumatology, Howard Hughes Medical Institute, Washington University School of Medicine, St. Louis, MO 63110

We have used a recombinant, biotinylated form of the mouse NK cell inhibitory receptor, Ly49A, to visualize the expression of MHC class I (MHC-I) ligands on living lymphoid cells. A panel of murine strains, including MHC congenic lines, was examined. We detected binding of Ly49A to cells expressing H-2Dd, H-2Dk, and H-2Dp but not to those expressing other MHC molecules. Cells of the MHC-recombinant strain B10.PL (H-2u) not only bound Ly49A but also inhibited cytolysis by Ly49A+ effector cells, consistent with the correlation of in vitro binding and NK cell function. Binding of Ly49A to H-2Dd-bearing cells of different lymphoid tissues was proportional to the level of H-2Dd expression and was not related to the lineage of the cells examined. These binding results, interpreted in the context of amino acid sequence comparisons and the recently determined three-dimensional structure of the Ly49A/H-2Dd complex, suggest a role for amino acid residues at the amino-terminal end of the {alpha}1 helix of the MHC-I molecule for Ly49A interaction. This view is supported by a marked decrease in affinity of an H-2Dd mutant, I52 M, for Ly49A. Thus, allelic variation of MHC-I molecules controls measurable affinity for the NK inhibitory receptor Ly49A and explains differences in functional recognition in different mouse strains.




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