The interchain disulfide linkage of T-cell antigen receptor-alpha and -beta chains is a prerequisite for T-cell activation

Complementary DNAs encoding the T-cell antigen receptor (TCR)-alpha and mut ant TCR-beta chains, lacking the interchain disulfide bond-related cysteine , were introduced into a TCR-alpha and -beta protein-deficient T-cell line. TCR-alpha and the mutant TCR-beta chains assembled with the CD3-epsilon, - gamma, -delta, and -zeta subunits and were efficiently transported to the c ell surface; however, the hybrid TCR molecules exhibited a diminished respo nse to T-cell activation by major histocompatibility complex-bound antigen, superantigen, and TCR crosslinking. These results suggest that the interch ain disulfide bond between the TCR clonotypic chains is not required for TC R assembly and cell surface expression, but it plays an important role in m aintaining the functional integrity of the TCR complex. (C) 1998 Academic P ress.