Journal
EUROPEAN JOURNAL OF IMMUNOLOGY
Volume 44, Issue 12, Pages 3508-3521Publisher
WILEY
DOI: 10.1002/eji.201444902
Keywords
Antigen presentation; Immunoproteasome; MHC class I restricted epitopes; Proteasome; Proteolysis
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Funding
- Deutsche Forschungsgemeinschaft [SFB 740, SFBTR43, DFG VO 1602/2-1, SFBTR 19 B3]
- BIH [CRG1-TP1]
- National Center for the Replacement Refinement & Reduction of Animals in Research (NC3Rs) through a David Sainsbury Fellowship
- BBSRC
- Leverhulme Trust
- Royal Society
- National Centre for the Replacement, Refinement and Reduction of Animals in Research (NC3Rs) [NC/K001949/1] Funding Source: researchfish
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Immunoproteasomes are considered to be optimised to process Ags and to alter the peptide repertoire by generating a qualitatively different set of MHC class I epitopes. Whether the immunoproteasome at the biochemical level, influence the quality rather than the quantity of the immuno-genic peptide pool is still unclear. Here, we quantified the cleavage-site usage by human standard-and immunoproteasomes, and proteasomes from immuno-subunit-deficient mice, as well as the peptides generated from model polypeptides. We show in this study that the different proteasome isoforms can exert significant quantitative differences in the cleavage-site usage and MHC class I restricted epitope production. However, independent of the proteasome isoform and substrates studied, no evidence was obtained for the abolishment of the specific cleavage-site usage, or for differences in the quality of the peptides generated. Thus, we conclude that the observed differences in MHC class I restricted Ag presentation between standard- and immunoproteasomes are due to quantitative differences in the proteasome-generated antigenic peptides.
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