Hepatitis C virus mutation affects proteasomal epitope processing
J. Clin. Invest. Ulrike Seifert, et al. 114:250 doi:10.1172/JCI20985 [Go to this article.]

Figure 4
Biochemical and immunological analysis of proteasomal digests. (A) NS31073–1081–specific CD8⁺ T cells lyse T2 cells loaded with either the NS31073–1081 serine variant SVNGVCWTV or the NS3_1073–1081 epitope CVNGVCWTV. (B–C) Generation of NS31073–1081 serine variant SVNGVCWTV from NS3(Wt)1062–1095 (filled circles) and NS3(Mut)_1062–1095 (open circles) serine variant polypeptides NS3_1062–1095 by digestion with constitutive 20S proteasome (B) and by digestion with 20S immunoproteasome (C). (D–E) 8-hour–proteasome (D) and immunoproteasome (E) digests of NS3(Wt)1062–1095 and NS3(Mut)1062–1095 serine variant polypeptides were loaded onto TAP-deficient T2-target cells and incubated with NS31073–1081 epitope–specific, cytotoxic T cells at an effector to target ratio of 13 to 1. For comparison, 10-⁵ M NS3_1073–1081 serine variant was loaded onto T2 target cells. Only wild-type and not the mutant polypeptide digests were recognized by NS3_1073–1081 epitope–specific cytotoxic T cells.