Proteasome subtypes and the processing of tumor antigens: increasing antigenic diversity

N Vigneron, BJ Van den Eynde - Current opinion in immunology, 2012 - Elsevier
N Vigneron, BJ Van den Eynde
Current opinion in immunology, 2012Elsevier
Protein degradation by the proteasome releases peptides that can be loaded on MHC class
I molecules and presented to cytolytic T lymphocytes. Several mechanisms were recently
found to increase the diversity of antigenic peptides displayed at the cell surface, thereby
maximizing the efficacy of immune responses. The proteasome was shown to produce
spliced antigenic peptides, which are made of two fragments initially not contiguous in the
parental protein. Different proteasome subtypes also produce distinct sets of antigenic …
Protein degradation by the proteasome releases peptides that can be loaded on MHC class I molecules and presented to cytolytic T lymphocytes. Several mechanisms were recently found to increase the diversity of antigenic peptides displayed at the cell surface, thereby maximizing the efficacy of immune responses. The proteasome was shown to produce spliced antigenic peptides, which are made of two fragments initially not contiguous in the parental protein. Different proteasome subtypes also produce distinct sets of antigenic peptides: the standard proteasome and the immunoproteasome, containing different catalytic subunits, have different cleavage specificities and produce different sets of peptides. Moreover, recent work confirmed the existence of two additional proteasome subtypes that are intermediate between the standard and the immunoproteasome, and each produce a unique peptide repertoire.
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