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Cutting Edge: HLA-B27 Acquires Many N-Terminal Dibasic Peptides: Coupling Cytosolic Peptide Stability to Antigen Presentation¹

Carla A. Herberts^*, Joost J. Neijssen^*, Jolanda de Haan^*, Lennert Janssen^*, Jan Wouter Drijfhout, Eric A. Reits^2,* and Jacques J. Neefjes^3,*

^* Division of Tumor Biology, The Netherlands Cancer Institute, Amsterdam, The Netherlands; and Department of Immunohematology and Blood Transfusion, Leiden University Medical Center, Leiden, The Netherlands

Ag presentation by MHC class I is a highly inefficient process because cytosolic peptidases destroy most peptides after proteasomal generation. Various mechanisms shape the MHC class I peptidome. We define a new one: intracellular peptide stability. Peptides with two N-terminal basic amino acids are more stable than other peptides. Such peptides should be overrepresented in the peptidome of MHC class I-associated peptides. HLA-B27 binding peptides use anchor residue R at P2 and, although most amino acids are allowed, particular amino acids are overrepresented at P1, including R and K. We show that such N-terminal dibasic peptides are indeed more efficiently presented by HLA-B27. This suggests that HLA-B27 can present peptides from Ags present in fewer copies than required for successful peptide generation for other MHC class I molecules.

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