Pleiotropic effects of post-translational modifications on the fate of viral glycopeptides as cytotoxic T cell epitopes

摘要: Abstract The fate of viral glycopeptides as cytotoxic T lymphocyte (CTL) epitopes is unclear. We have dissected the mechanisms antigen presentation and CTL recognition peptide GP392–400 (WLVTNGSYL) from lymphocytic choriomeningitis virus (LCMV) compared them with those previously reported GP92–101 (CSANNSHHYI). Both bear a glycosylation motif, are naturallyN-glycosylated in mature glycoproteins, bind to major histocompatibility complex H-2Db molecules, immunogenic. However, post-translational modifications differentially affected GP392–400. Upon N-glycosylation or de-N-glycosylation, marked decrease binding was observed for but not GP92–101. Further, under its N-glycosylated de-N-glycosylated form, then lost initial ability generate response mice, whereas still immunogenic same conditions. genetically encoded form GP392–400, which on basis immunogenicity could be presented during course LCMV infection, does fact appear at surface LCMV-infected cells. Our results show that can pleiotropic effects their by contribute either creation neo-epitopes destruction potential epitopes.