Why do proteases mess up with antigen presentation by re-shuffling antigen sequences?. (June 2018)

• Record Type: Journal Article
• Authors: Liepe, Juliane; Ovaa, Huib; Mishto, Michele
• Is Part Of: Current opinion in immunology. Volume 52(2018)
• Page Start: 81
• Page End: 86
• Publication Date: 2018-06
• Subjects: Immunology -- Periodicals; Allergy -- Periodicals; Immunology -- Abstracts -- Periodicals; Allergy -- Abstracts -- Periodicals; 616.079
• DOI: 10.1016/j.coi.2018.04.016
• Languages: English
• ISSNs: 0952-7915

Abstract

Highlights: Non-canonical epitopes have emerged as large part of immunopeptidomes. Spliced peptides represent 20–30% of the MHC-I immunopeptidome variety. Peptide splicing by proteasome and other proteases is regulated and efficient. Peptide splicing efficiency can have implications in defining the immunological self. Abstract : The sequence of a large number of MHC-presented epitopes is not present as such in the original antigen because it has been re-shuffled by the proteasome or other proteases. Why do proteases throw a spanner in the works of our model of antigen tagging and immune recognition? We describe in this review what we know about the immunological relevance of post-translationally spliced epitopes and why proteases seem to have a second (dark) personality, which is keen to create new peptide bonds.