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CUTTING EDGE |
*
La Jolla Institute for Allergy and Immunology, San Diego, CA 92121; and
Pharmaceutical Research Laboratory, Kirin Brewery, Gunma, Japan
The reactivity of a group of mouse V
14+ NK T cell
hybridomas was tested with a panel of analogs of the glycolipid
-galactosylceramide (-GalCer). Interestingly, the nearly complete
truncation of the acyl chain from 24 to 2 carbons does not
significantly affect the mouse NK T cell response to glycolipid
presented by either mouse CD1 (mCD1) or its human homolog CD1d
(hCD1d). Therefore, we propose that only one of the two hydrophobic
pockets of the CD1 Ag-binding groove needs to be filled by Ag. In terms
of the sphingosine base, the mCD1 binding groove has less-demanding
structural requirements for presentation to NK T cells than hCD1d.
Tests of NK T cell reactivity to analogs presented by hCD1d
demonstrates that the invariant TCRs expressed by mouse and human NK T
cells are surprisingly similar in their requirements for glycolipid
recognition.
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