The TCP-1 Ring Complex (TRiC) binds antigenic peptides and facilitates their cross-presentation by APCs (93.5)

Abstract

Abstract The multimeric chaperonin TCP-1 Ring Complex (TRiC), an hsp60 homologue, was recently found to associate with the precursors of the ovalbumin-derived SIINFEKL epitope during processing and loading onto MHC I. The TRiC-peptide association is essential for loading of MHC I. Here, we have sought to characterize the peptide-binding properties of TRiC in vitro, and study the behavior of TRiC-peptide complexes in cross-presentation assays. TRiC is shown to bind a variety of peptides in vitro in much the same manner as previously described peptide chaperones of the hsp90 family. TRiC-peptide complexes are efficiently taken up by APCs and the peptides are processed and represented on MHC class I for recognition by specific CD8+ T cells. These results as well as the immunological properties of TRiC-peptide complexes formed in vivo shall be reported.