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CUTTING EDGE |
Domain on the Avidity of CD1d:
-Galactosylceramide Binding by Invariant V14 NKT Cells1
* Ludwig Institute for Cancer Research, Lausanne Branch, Epalinges, Switzerland; and
BD Biosciences PharMingen, San Diego, CA 92121
CD1d tetramers loaded with 
-galactosylceramide (-GalCer) bind selectively to mouse invariant V14 (V14i) NKT cells and their human counterparts. Whereas tetramer binding strictly depends on the expression of a V14-J18 chain in murine NKT cells, the associated 
-chain (typically expressing V8.2 or V7) appears not to influence tetramer binding. In this study, we describe novel -GalCer-loaded mouse and human CD1d-IgG1 dimers, which revealed an unexpected influence of the TCR- chain on the avidity of CD1d:-GalCer binding. A subset of V14i NKT cells clearly discriminated -GalCer bound to mouse or human CD1d on the basis of avidity differences conferred by the V domain of the TCR- chain, with V8.2 conferring higher avidity binding than V7.
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