DIMERIZATION OF SOLUBLE MAJOR HISTOCOMPATIBILITY COMPLEX PEPTIDE COMPLEXES IS SUFFICIENT FOR ACTIVATION OF T-CELL HYBRIDOMA AND INDUCTION OF UNRESPONSIVENESS
Jp. Abastado et al., DIMERIZATION OF SOLUBLE MAJOR HISTOCOMPATIBILITY COMPLEX PEPTIDE COMPLEXES IS SUFFICIENT FOR ACTIVATION OF T-CELL HYBRIDOMA AND INDUCTION OF UNRESPONSIVENESS, The Journal of experimental medicine, 182(2), 1995, pp. 439-447
Major histocompatibility complex (MHC) class I molecules are cell-surf
ace proteins that present peptides to CD8(+) T cells. These peptides a
re mostly derived from endogenously synthesized protein. Recombinant,
soluble MHC class I molecules were produced, purified, and loaded homo
geneously with synthetic peptide. These MHC-peptide complexes were use
d to activate a T cell hybridoma. While monomers of MHC-peptide bound
to the T cell, they showed no stimulatory activity. Dimers fully trigg
ered the T cell hybridoma to secrete interleukin 2. This response was
followed by a state in which the T cell was refractory to restimulatio
n as a result of defective signal transduction through the T cell rece
ptor.