Glycoprotein 96 Can Chaperone Both MHC Class I- and Class II-Restricted Epitopes for In Vivo Presentation, but Selectively Primes CD8+ T Cell Effector Function

摘要: The ability of mature T lymphocytes to develop effector capacity after encounter with cognate Ag is generally dependent upon inflammatory signals associated infection that induce dendritic cell activation/maturation. These can derive directly from pathogens or be expressed by host cells in response infection. Heat shock proteins (HSPs) are a class host-derived mediators perform the duel function both chaperoning MHC I-restricted epitopes into cross-presentation pathway DCs and inducing activation/maturation these allow priming CD8+ responses. Although HSPs elicit CD8 responses has been well established, their potential prime CD4 relatively unexplored. In current study we compared endoplasmic reticulum-resident HSP gp96 vs using TCR transgenic adoptive transfer systems soluble gp96-peptide complexes. As expected, facilitated peptide cells. Interestingly, also vivo presentation II-restricted peptide; however, resulting did not involve development function. Taken together, data suggest an mediator selectively primes