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The proteasome is the major protease responsible for the production of antigenic peptides recognized by CD8+ cytolytic T cells (CTL). These peptides, generally 8-10 amino acids long, are presented at the cell surface by major histocompatibility complex (MHC) class I molecules. Originally, these peptides were believed to be solely derived from linear fragments of proteins, but this concept was challenged several years ago by the isolation of anti-tumor CTL that recognized spliced peptides, i.e. peptides composed of fragments distant in the parental protein. The splicing process was shown to occur in the proteasome through a transpeptidation reaction involving an acyl-enzyme intermediate. Here, we review the steps that led to the discovery of spliced peptides as well as the recent advances that uncover the unexpected importance of spliced peptides in the composition of the MHC class I repertoire.

Original publication

DOI

10.1074/jbc.R117.807560

Type

Journal article

Journal

J Biol Chem

Publication Date

22/12/2017

Volume

292

Pages

21170 - 21179

Keywords

MHC class I, antigen presentation, antigen processing, cytolytic T lymphocytes, major histocompatibility complex (MHC), peptides, proteasome, spliced peptides