Abstract:
:CD8+ cytolytic T lymphocytes are essential players of anti-tumor immune responses. On tumors, they recognize peptides of about 8-to-10 amino acids that generally result from the degradation of cellular proteins by the proteasome. Until a decade ago, these peptides were thought to solely correspond to linear fragments of proteins that were liberated after the hydrolysis of the peptide bonds located at their extremities. However, several examples of peptides containing two fragments originally distant in the protein sequence challenged this concept and demonstrated that proteasome could also splice peptides together by creating a new peptide bond between two distant fragments. Unexpectedly, peptide splicing emerges as an essential way to increase the peptide repertoire diversity as these spliced peptides were shown to represent up to 25% of the peptides presented on a cell by MHC class I. Here, we review the different steps that led to the discovery of peptide splicing by the proteasome as well as the lightening offered by the recent progresses of mass spectrometry and bioinformatics in the analysis of the spliced peptide repertoire.
journal_name
Mol Immunoljournal_title
Molecular immunologyauthors
Vigneron N,Stroobant V,Ferrari V,Abi Habib J,Van den Eynde BJdoi
10.1016/j.molimm.2018.03.030subject
Has Abstractpub_date
2019-09-01 00:00:00pages
93-102eissn
0161-5890issn
1872-9142pii
S0161-5890(18)30109-3journal_volume
113pub_type
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