Using intein catalysis to probe the origin of major histocompatibility complex class I-presented peptides.

ABSTRACT: All vertebrate nucleated cells generate peptides from their expressed gene products and then display them at the cell surface bound to MHC class I molecules. This allows CD8(+) T cells to detect and eliminate abnormal cells that are synthesizing foreign proteins, e.g., from viruses or mutations. To permit the immune system to more uniformly monitor a cell's proteins, regardless of their half-life or location, it has been thought that the products of rapid degradation of the mistakes of protein synthesis (defective ribosomal products, DRiPs) preferentially contribute to the class I-presented peptides. However, using intein catalysis to generate peptide sequences exclusively by posttranslational splicing of mature proteins, we show here that presented peptides can be generated from fully fol

SUBMITTER: Farfan-Arribas DJ 

PROVIDER: S-EPMC3479494 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature