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*
Department of Immunohematology and Blood Bank, Leiden University Medical Center, Leiden, The Netherlands;
Division of Tumor Biology, The Netherlands Cancer Institute, Amsterdam, The Netherlands; and
Institute of Biochemistry, Charité, Humboldt University, Berlin, Germany
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 processing of the Friend epitope which is due to a
single amino acid substitution (N
D) immediately flanking the
C-terminal anchor residue of the epitope. Proteasome-mediated digestion
analysis of a synthetic 26-mer peptide derived from the Friend sequence
shows that cleavage takes place predominantly C-terminal of D, instead
of V as is the case for the Moloney MuLV sequence. Therefore, the C
terminus of the epitope is not properly generated. Epitope-containing
peptide fragments extended with an additional C-terminal D are not
efficiently translocated by TAP and do not show significant binding
affinity to MHC class I-Kb molecules. Thus, a potential CTL
epitope present in the Friend virus sequence is not properly processed
and presented because of a natural flanking aspartic acid that
obliterates the correct C-terminal cleavage site. This constitutes a
novel way to subvert proteasome-mediated generation of proper antigenic
peptide fragments.
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