The adaptive immune response depends on the creation of suitable peptides from foreign antigens for display on MHC molecules to T lymphocytes. Similarly, MHC-restricted display of peptides derived from self proteins results in the elimination of many potentially autoreactive T cells. Different proteolytic systems are used to generate the peptides that are displayed as T cell epitopes on class I compared with class II MHC molecules. In the case of class II MHC molecules, the proteases that reside within the endosome/lysosome system of antigen-presenting cells are responsible; surprisingly, however, there are relatively few data on which enzymes are involved. Recently we have asked whether proteolysis is required simply in a generic sense, or whether the action of particular enzymes is needed to generate specific class II MHC-associated T cell epitopes. Using the recently identified mammalian asparagine endopeptidase as an example, we review recent evidence that individual enzymes can make clear and non-redundant contributions to MHC-restricted peptide display.
Roles for asparagine endopeptidase in class II MHC-restricted antigen processing
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Jeremy Saklatvala, Hideaki Nagase, Guy Salvesen, Colin Watts, Daniela Mazzeo, Michelle A. West, Stephen P. Matthews, Doreen Keane, Garth Hamilton, Linda V. Persson, Jennifer M. Lawson, Bénédicte Manoury, Catherine X. Moss; Roles for asparagine endopeptidase in class II MHC-restricted antigen processing. Biochem Soc Symp 1 September 2003; 70 31–38. doi: https://doi.org/10.1042/bss0700031
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