Nature 356, 793 - 796 (30 April 1992); doi:10.1038/356793a0

Specific low-affinity recognition of major histocompatibility complex plus peptide by soluble T-cell receptor

Susanna Weber, André Traunecker, Filippo Oliveri, Walter Gerhard^* & Klaus Karjalainen

The Basel Institute for Immunology, Grenzacherstrasse 487, Postfach CH-4005 Basel, Switzerland
^* The Wistor Institute of Anatomy and Biology, 36th Street at Spruce, Philadelphia, Pennsylvania 19104, USA

THE T-cell receptor is necessary and sufficient for recognition of peptides presented by major histocompatibility complex molecules^1,2. Other adhesion molecules, like CD4 or CDS, play an auxiliary role in antigen recognition by T cells^3,4. Here we analyse T-cell receptor (TCR) binding using a soluble rather than a cell-bound receptor molecule. A TCR-immunoglobulin chimaera is constructed with the variable and the first constant regions of both the TCR - and-chains linked to the immunoglobulin light-chain constant regions. This soluble TCR is expressed, assembled and secreted as an heterodimer by a myeloma cell line transfected with the recombinant genes. Furthermore, the soluble TCR is biologically active: it specifically inhibits antigen-dependent activation of the relevant T-cell clones and thus discriminates between proper and irrelevant peptides presented by major histocompatibility complex molecules.

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