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*
Molecular Biology Section, Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892;
Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Cientificas, Campus de la Universidad Autónoma de Madrid, Madrid, Spain;
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
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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