Cutting Edge: Influence of the TCR Vβ Domain on the Avidity of CD1d:α-Galactosylceramide Binding by Invariant Vα14 NKT Cells
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- Jens Schümann
- *Ludwig Institute for Cancer Research, Lausanne Branch, Epalinges, Switzerland; and
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- Roger B. Voyle
- *Ludwig Institute for Cancer Research, Lausanne Branch, Epalinges, Switzerland; and
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- Bing-Yuan Wei
- † BD Biosciences PharMingen, San Diego, CA 92121
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- H. Robson MacDonald
- *Ludwig Institute for Cancer Research, Lausanne Branch, Epalinges, Switzerland; and
抄録
<jats:title>Abstract</jats:title> <jats:p>CD1d tetramers loaded with α-galactosylceramide (α-GalCer) bind selectively to mouse invariant Vα14 (Vα14i) NKT cells and their human counterparts. Whereas tetramer binding strictly depends on the expression of a Vα14-Jα18 chain in murine NKT cells, the associated β-chain (typically expressing Vβ8.2 or Vβ7) appears not to influence tetramer binding. In this study, we describe novel α-GalCer-loaded mouse and human CD1d-IgG1 dimers, which revealed an unexpected influence of the TCR-β chain on the avidity of CD1d:α-GalCer binding. A subset of Vα14i NKT cells clearly discriminated α-GalCer bound to mouse or human CD1d on the basis of avidity differences conferred by the Vβ domain of the TCR-β chain, with Vβ8.2 conferring higher avidity binding than Vβ7.</jats:p>
収録刊行物
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- The Journal of Immunology
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The Journal of Immunology 170 (12), 5815-5819, 2003-06-15
The American Association of Immunologists