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© The Rockefeller University Press, 0022-1007/1998/5/1529/ $5.00
The Journal of Experimental Medicine, Volume 187, Number 9, May 4, 1998 1529-1536

Articles

One of the CD3{varepsilon} Subunits within a T Cell Receptor Complex Lies in Close Proximity to the Cβ FG Loop

Yoseph Ghendler, Alex Smolyar, Hsiu-Ching Chang, and Ellis L. Reinherz

From the Laboratory of Immunobiology, Dana-Farber Cancer Institute and Department of Medicine, Harvard Medical School, Boston, Massachusetts 02115

A recent crystal structure of the N15 {alpha}/β-T cell receptor (TCR) in complex with an Fab derived from the H57 Cβ-specific monoclonal antibody (mAb) shows the mAb fragment interacting with the elongated FG loop of the Cβ domain. This loop creates one side wall of a cavity within the TCR Ti-{alpha}/β constant region module (C{alpha}Cβ) while the CD and EF loops of the C{alpha} domain form another wall. The cavity size is sufficient to accommodate a single nonglycosylated Ig domain such as the CD3{varepsilon} ectodomain. By using specific mAbs to mouse TCR-β (H57) and CD3{varepsilon} (2C11) subunits, we herein provide evidence that only one of the two CD3{varepsilon} chains within the TCR complex is located in close proximity to the TCR Cβ FG loop, in support of the above notion. Moreover, analysis of T cells isolated from transgenic mice expressing both human and mouse CD3{varepsilon} genes shows that the heterologous human CD3{varepsilon} component can replace the mouse CD3{varepsilon} at this site. The location of one CD3{varepsilon} subunit within the rigid constant domain module has implications for the mechanism of signal transduction throughout T cell development.

Address correspondence to Ellis L. Reinherz, Laboratory of Immunobiology, Dana-Farber Cancer Institute, Boston, MA 02115. Phone: 617-632-3412; Fax: 617-632-3351; E-mail: ellis_reinherz{at}dfci.harvard.edu

Abbreviations used: DN, double negative; DP, double positive; mFI, mean fluorescence intensity; pT{alpha}, pre-T{alpha}; tg, transgenic; WT, wild-type.


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