Journal
JOURNAL OF IMMUNOLOGY
Volume 169, Issue 3, Pages 1340-1348Publisher
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.169.3.1340
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Funding
- NCI NIH HHS [R01 CA52511] Funding Source: Medline
- NIAID NIH HHS [R01 AI45053, R01 AI48540] Funding Source: Medline
- NIGMS NIH HHS [R01 U54GM62116, R01 GM48002, R01 GM39476] Funding Source: Medline
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Most CD1d-dependent NKT cells in mice have a canonical Valpha14Jalpha18 TCR rearrangement. However, relatively little is known concerning the molecular basis for their reactivity to glycolipid Ags presented by CD1d. Using glycollpid Ags, soluble forms of a Valpha14 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 a-helical amino acids could be defined that do not greatly alter lipid binding, but that affect the interaction with the TCR. Binding of the Valpha14(+) TCR to CD1d requires the agonist alpha-galactosyleeramide (alpha-GalCer), as opposed to the nonantigenic beta-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 alpha-GalCer/CD1d complex, with a particularly slow off rate. These unique properties are consistent with the coreceptor-independent action of the Va14 TCR and may be related to the intense response to a-GalCer by NKT cells in vivo.
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