Abrogation of CTL epitope processing by single amino acid substitution flanking the C-terminal proteasome cleavage site.

@article{Beekman2000AbrogationOC,
  title={Abrogation of CTL epitope processing by single amino acid substitution flanking the C-terminal proteasome cleavage site.},
  author={Nico J. C. M. Beekman and Peter A. van Veelen and Thorbald van Hall and Anne Neisig and Alice J. A. M. Sijts and Marcel G. M. Camps and Peter Michael Kloetzel and Jacques Neefjes and Cornelis J M Melief and Ferry A. Ossendorp},
  journal={Journal of immunology},
  year={2000},
  volume={164 4},
  pages={1898-905}
}
CTL directed against the Moloney murine leukemia virus (MuLV) epitope SSWDFITV recognize Moloney MuLV-induced tumor cells, but do not recognize cells transformed by the closely related Friend MuLV. The potential Friend MuLV epitope has strong sequence homology with Moloney MuLV and only differs in one amino acid within the CTL epitope and one amino acid just outside the epitope. We now show that failure to recognize Friend MuLV-transformed tumor cells is based on a defect in proteasome-mediated… CONTINUE READING

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