Cutting edge:: Influence of the TCR Vβ domain on the avidity of CD1d:α-galactosylceramide binding by invariant Vα14 NKT cells

被引：68

作者：

Schümann, J

Voyle, RB

Wei, BY

MacDonald, HR

机构：

[1] Ludwig Inst Canc Res, Lausanne Branche, CH-1066 Epalinges, Switzerland

[2] BD Biosci Pharmingen, San Diego, CA 92121 USA

来源：

JOURNAL OF IMMUNOLOGY | 2003年 / 170卷 / 12期

关键词：

D O I：

10.4049/jimmunol.170.12.5815

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

CD1d tetramers loaded with alpha-galactosylceramide (alpha-GalCer) hind selectively to mouse invariant Valpha14 (Valpha14i) NKTcells and their human counterparts. Whereas tetramer binding strictly depends on the expression of a Valpha14-Jalpha18 chain in murine NKT cells, the associated beta-chain (typically expressing Vbeta8.2 or Vbeta7) appears not to influence tetramer binding. In this study, we describe novel alpha-GalCer-loaded mouse and human CD1d-IgG1 dimers, which revealed an unexpected influence of the TCR-beta chain on the avidity of CD1d-alpha-GalCer binding. A subset of Valpha14i NKT cells clearly discriminated alpha-GalCer hound to mouse or human CD1d on the basis of avidity differences conferred by the Vbeta domain of the TCR-beta chain, with Vbeta8.2 conferring higher avidity binding than Vbeta7.

引用

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页码：5815 / 5819

页数：5

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