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A Role for the -Chain Connecting Peptide Motif in Mediating TCR-CD8 Cooperation

Dieter Naeher^*, Immanuel F. Luescher and Ed Palmer^1,*

^* Laboratory of Transplantation Immunology and Nephrology, University Hospital, Basel, Switzerland; and Ludwig Institute for Cancer Research, Lausanne Branch, University of Lausanne, Epalinges, Switzerland

To generate peripheral T cells that are both self-MHC restricted and self-MHC tolerant, thymocytes are subjected to positive and negative selection. How the TCR discriminates between positive and negative selection ligands is not well understood, although there is substantial evidence that the CD4 and CD8 coreceptors play an important role in this cell fate decision. We have previously identified an evolutionarily conserved motif in the TCR, the -chain connecting peptide motif (-CPM), which allows the TCR to deliver positive selection signals. Thymocytes expressing -CPM-deficient receptors do not undergo positive selection, whereas their negative selection is not impaired. In this work we studied the ligand binding and receptor function of -CPM-deficient TCRs by generating T cell hybridomas expressing wild-type or -CPM-deficient forms of the T1 TCR. This K^d-restricted TCR is specific for a photoreactive derivative of the Plasmodium berghei circumsporozoite peptide_252–260 IASA-YIPSAEK(ABA)I and is therefore amenable to TCR photoaffinity labeling. The experiments presented in this work show that -CPM-deficient TCRs fail to cooperate with CD8 to enhance ligand binding and functional responses.

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