[HTML][HTML] Targeting of EBNA1 for rapid intracellular degradation overrides the inhibitory effects of the Gly-Ala repeat domain and restores CD8+ T cell recognition
Epstein-Barr virus (EBV)-encoded nuclear antigen 1 (EBNA1) includes a unique glycine-
alanine repeat domain that inhibits the endogenous presentation of cytotoxic T lymphocyte
(CTL) epitopes through the class I pathway by blocking proteasome-dependent degradation
of this antigen. This immune evasion mechanism has been implicated in the pathogenesis of
EBV-associated diseases. Here, we show that cotranslational ubiquitination combined with
N-end rule targeting enhances the intracellular degradation of EBNA1, thus resulting in a …
alanine repeat domain that inhibits the endogenous presentation of cytotoxic T lymphocyte
(CTL) epitopes through the class I pathway by blocking proteasome-dependent degradation
of this antigen. This immune evasion mechanism has been implicated in the pathogenesis of
EBV-associated diseases. Here, we show that cotranslational ubiquitination combined with
N-end rule targeting enhances the intracellular degradation of EBNA1, thus resulting in a …