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14 NKT Cell TCR Exhibits High-Affinity Binding to a Glycolipid/CD1d Complex1
* Division of Developmental Immunology, La Jolla Institute for Allergy and Immunology, San Diego, CA 92121;
Department of Immunology, The Scripps Research Institute, La Jolla, CA 92037; and
Departments of Microbiology and Immunology and Structural Biology, Stanford University School of Medicine, Stanford, CA 94305
Most CD1d-dependent NKT cells in mice have a canonical V
14J18
TCR rearrangement. However, relatively little is known concerning the
molecular basis for their reactivity to glycolipid Ags presented by
CD1d. Using glycolipid Ags, soluble forms of a V14 NKT cell-derived
TCR, and mutant and wild-type CD1d molecules, we probed the TCR/CD1d
interaction by surface plasmon resonance, tetramer equilibrium
staining, and tetramer staining decay experiments. By these methods,
several CD1d -helical amino acids could be defined that do not
greatly alter lipid binding, but that affect the interaction with the
TCR. Binding of the V14+ TCR to CD1d requires the
agonist -galactosylceramide (-GalCer), as opposed to the
nonantigenic 
-galactosylceramide, although both Ags bind to CD1d,
indicating that the carbohydrate moiety of the CD1d-bound Ag plays a
major role in the TCR interaction. The TCR has a relatively
high-affinity binding to the -GalCer/CD1d complex, with a
particularly slow off rate. These unique properties are consistent with
the coreceptor-independent action of the V14 TCR and may be related
to the intense response to -GalCer by NKT cells in
vivo.
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