Specificity and binding properties of a single-chain T cell receptor

Journal of Molecular Biology
C J SchlueterDavid M Kranz

Abstract

The specificity of a T cell is dictated by an alpha beta T cell receptor (TCR) that recognizes a complex of peptide and a product of the major histocompatibility complex (MHC). Recent studies have begun to characterize the affinities and kinetics of these interactions, but details of the alpha beta TCR structure and function are not known. To examine some of these issues we focus in this report on a TCR derived from the T cell clone 2C. This TCR binds to a complex of the nonapeptide QL9 and the class I MHC product Ld with the highest affinity of any known TCR/ligand interaction (KD approximately 10 (-7) M). Circular dichroism showed that a single-chain TCR (scTCR) containing linked V alpha and V beta regions from T cell 2C and refolded from Escherichia coli inclusion bodies exhibited the characteristic beta-sheet structure of immunoglobulins. A sensitive assay that is capable of detecting the interaction of soluble scTCR with peptide /MHC ligand on the surface of target cells was used to demonstrate that the peptide specificity of this scTCR reflects that of the TCR found on the surface of 2C. Analysis of several scTCR V alpha region mutants confirmed that the V alpha domain is critical for the specificity of scTCR binding. Fin...Continue Reading

Citations

Oct 1, 1996·The Journal of Experimental Medicine·D PlaksinD H Margulies
Jun 8, 1999·Annual Review of Immunology·K C GarciaI A Wilson
Feb 12, 1998·Proceedings of the National Academy of Sciences of the United States of America·K C GarciaL Teyton
Aug 5, 2000·Journal of Immunotherapy·A CalogeroG A Hospers
May 13, 1999·Proceedings of the National Academy of Sciences of the United States of America·M C KiekeD M Kranz

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