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Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rockville, MD 20852
The 
2 integrin LFA-1 (CD11a/CD18) mediates adhesion
of lymphocytes to cells expressing ICAM. The strength of this adhesion
is regulated by different signals delivered by cytokines and
chemokines, and by the TCR in the case of T cells. To determine the
receptor-ligand interactions required for adhesion of resting NK cells,
Drosophila cells expressing different combinations of
ligands of human NK cell receptors were generated. Expression of
ICAM-1 alone was sufficient for an adhesion of resting NK cells that
was sensitive to inhibitors of src family kinase and of
phosphatidylinositol 3-kinase. Binding of resting NK cells to
solid-phase ICAM-1 showed similar signaling requirements. A pulse of
either IL-2 or IL-15 to resting NK cells resulted in strongly enhanced,
actin-dependent adhesion to insect cells expressing ICAM-1 alone.
Coexpression of either LFA-3 (CD58) or CD48 with ICAM-1 resulted in
strong adhesion by resting NK cells, even in the absence of cytokines.
Therefore, receptors for LFA-3 and CD48 on resting NK cells strengthen
the adhesion mediated by LFA-1.
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