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TY - JOUR AU - Weber, Susanna AU - Traunecker, André AU - Oliveri, Filippo AU - Gerhard, Walter AU - Karjalainen, Klaus PY - 1992 DA - 1992/04/01 TI - Specific low-affinity recognition of major histocompatibility complex plus peptide by soluble T-cell receptor JO - Nature SP - 793 EP - 796 VL - 356 IS - 6372 AB - THE T-cell receptor is necessary and sufficient for recognition of peptides presented by major histocompatibility complex molecules1,2. Other adhesion molecules, like CD4 or CDS, play an auxiliary role in antigen recognition by T cells3,4. 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 α- andβ-chains linked to the immunoglobulin light-chain constant regions. This soluble TCR is expressed, assembled and secreted as an αβ 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. SN - 1476-4687 UR - https://doi.org/10.1038/356793a0 DO - 10.1038/356793a0 ID - Weber1992 ER -