The Journal of Experimental Medicine
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© The Rockefeller University Press, 0022-1007/1997/12/1933/ $5.00
The Journal of Experimental Medicine, Volume 186, Number 11, December 1, 1997 1933-1938

Brief Definitive Reports

Signaling Efficiency of the T Cell Receptor Controlled by a Single Amino Acid in the β Chain Constant Region

B. Thomas Bäckström, Barbara T. Hausmann, and Ed Palmer

From the Basel Institute for Immunology, CH-4005 Basel, Switzerland

A single amino acid residue, Gln136, located within the connecting peptide domain of Cβ controls the ability of the {alpha}/β TCR to transmit a full signal. TCRs in which this Cβ residue is mutated to Phe, the residue found in TCR-{gamma}, are unresponsive to antigenic ligands. Interestingly, this Cβ residue is either polar or charged in every species studied thus far, including the trout and the skate. In contrast, the analogous residue in C{gamma} is always hydrophobic. In spite of their compromised antigen responsiveness, the mutant TCR complex contains the CD3-{gamma}, -{delta}, -{varepsilon}, and -{zeta} chains, and undergoes {zeta} chain phosphorylation and ZAP-70 recruitment. However, the biological response of the mutant TCR could be rescued with a calcium ionophore, implying that mutant TCRs are defective in generating a calcium-mediated signal. The implications of the differences between Cβ and C{gamma} are considered.

Address correspondence to Dr. Ed Palmer, Basel Institute for Immunology, Grenzacherstrasse 487, CH-4005 Basel, Switzerland. Phone: 41-61-605-1277; FAX: 41-61-605-1364; E-mail: Palmer{at}bii.ch B. Thomas Bäckström's current address is Malaghan Institute of Medical Research, PO Box 7060, Wellington South, New Zealand.

The Basel Institute for Immunology was founded and is supported by F. Hoffmann-La Roche LTD, Basel, Switzerland.


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