Roles for asparagine endopeptidase in class II MHC-restricted antigen processing

Colin Watts (Lead / Corresponding author), Daniela Mazzeo, Michelle A. West, Stephen P. Matthews, Doreen Keane, Garth Hamilton, Linda V. Persson, Jennifer M. Lawson, Bénédicte Manoury, Catherine X. Moss

    Research output: Contribution to journalArticlepeer-review

    5 Citations (Scopus)


    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.

    Original languageEnglish
    Pages (from-to)31-38
    Number of pages8
    JournalBiochemical Society Symposium
    Publication statusPublished - Sept 2003

    ASJC Scopus subject areas

    • Biochemistry


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