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The Journal of Immunology, 2002, 169: 4161-4171.
Copyright © 2002 by The American Association of Immunologists

The Final N-Terminal Trimming of a Subaminoterminal Proline-Containing HLA Class I-Restricted Antigenic Peptide in the Cytosol Is Mediated by Two Peptidases1

Frédéric Lévy2,3,*, Lena Burri2,*, Sandra Morel4,{dagger}, Anne-Lise Peitrequin*, Nicole Lévy{ddagger}, Angela Bachi§, Ulf Hellman, Benoît J. Van den Eynde{dagger} and Catherine Servis{ddagger}

* Ludwig Institute for Cancer Research, Lausanne Branch, and {dagger} Institute of Biochemistry, University of Lausanne, Epalinges, Switzerland; {ddagger} Ludwig Institute for Cancer Research, Brussels Branch, Université Catholique de Louvain, Brussels, Belgium; § DIBIT, San Raffaele Scientific Institute, Milan, Italy; and Ludwig Institute for Cancer Research, Uppsala Branch, Biomedical Center, Uppsala, Sweden

The proteasome produces MHC class I-restricted antigenic peptides carrying N-terminal extensions, which are trimmed by other peptidases in the cytosol or within the endoplasmic reticulum. In this study, we show that the N-terminal editing of an antigenic peptide with a predicted low TAP affinity can occur in the cytosol. Using proteomics, we identified two cytosolic peptidases, tripeptidyl peptidase II and puromycin-sensitive aminopeptidase, that trimmed the N-terminal extensions of the precursors produced by the proteasome, and led to a transient enrichment of the final antigenic peptide. These peptidases acted either sequentially or redundantly, depending on the extension remaining at the N terminus of the peptides released from the proteasome. Inhibition of these peptidases abolished the CTL-mediated recognition of Ag-expressing cells. Although we observed some proteolytic activity in fractions enriched in endoplasmic reticulum, it could not compensate for the loss of tripeptidyl peptidase II/puromycin-sensitive aminopeptidase activities.




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