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The number of T cell receptors on CTL clone 2C that are required for recognition of various peptide-MHC or superantigen-MHC ligands were measured as a function of both the ligand density on target cells and the binding affinity of the TCR. Quantitative inverse correlations were determined between the number of TCRs required for recognition and the number of(More)
The TCR from the alloreactive clone 2C recognizes p2C (LSPFPFDL)/Ld and QL9 (QLSPFPFDL)/Ld complexes with affinities of 2 x 10(6) and 10(7) M(-1). Recently, it was proposed that the Phe at position 4 of p2C is critical for recognition by the 2C TCR. To further characterize the role of this peptide position in binding to Ld and in recognition by the 2C TCR,(More)
The antigen-specific function of T cells is mediated through a surface receptor (alpha beta). Antibodies to the receptor can either inhibit or activate the T cell depending on the multimeric form of the antibody and the isotype of the antibody constant regions. To further examine and eventually control these antagonistic properties, an anti-receptor(More)
The diversity and domain structure of alpha beta T cell receptors (TCR) are similar to immunoglobulins based on sequence homologies, but the three-dimensional structure of the alpha beta-heterodimer has not been solved. To begin structure/function studies, we have compared the properties of a soluble single-chain V alpha V beta TCR (scTCR) expressed in(More)
Recent advances in the expression of Abs in Escherichia coli have raised the possibility that virtually any specificity can be obtained by either cloning Ab genes from characterized hybridomas or by de novo selection using Ab gene libraries. Bispecific Abs have been more difficult to engineer because of problems inherent in the proper folding and(More)
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(More)
In this report the VH and VL genes of the anti-T cell receptor (TCR) antibody KJ16, which recognizes the TCR V beta 8.1 and V beta 8.2 regions in mice, were cloned and expressed as a single-chain antibody (scFv) in Escherichia coli. A 29-kDa protein was obtained after renaturation from inclusion bodies. The KJ16 scFv had a relative affinity for the native(More)
In this study we present a strategy for the identification of novel peptide conjugates which may be used to understand the molecular details of the recognition process or to potentially regulate T cell-mediated responses. The approach involves the incorporation of cysteine into a known peptide at a position of interest and subsequent chemical conjugation(More)
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