12/17/2023 0 Comments Has many complex proteins and so have a robust system for heat-shock protein assisted folding![]() Immunogenicity of TRiC purified from OVA- or β-galactosidase–expressing cells, that is, of endogenously generated TRiC-peptide complexes, was investigated, and such preparations were observed not to be immunogenic. Mechanistic dissection of this phenomenon shows that TRiC binds APC, and TRiC-chaperoned peptides are processed within the APC and presented on their MHC class I. Immunization of mice with noncovalent complexes of peptides (derived from OVA or β-galactosidase) and TRiC results in cross-priming of CD8 + T lymphocytes specific for K b/SIINFEKL or L d/TPHPARIGL. We demonstrate in this study that purified TRiC binds antigenic peptides in vitro as well however, such binding is not restricted to N-terminally extended peptides, suggesting that the results obtained in vivo reflect the availability of peptides in vivo rather than structural constraints of TRiC-peptide binding. Binding of peptides to TRiC was shown to be essential for their presentation on MHC class I. The tailless complex polypeptide-1 ring complex (TRiC) is a eukaryotic heat shock protein 60 (hsp60) molecule that has been shown to bind N-terminally extended precursors of OVA-derived SIINFEKL in vivo.
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