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Major histocompatibility complex (MHC-I) peptide antigen processing and presentation has experienced a revived interest in the context of immuno oncology, immune surveillance escape by pathogen mutations and technical advances that accelerate vaccine design. This sheds new light on the discoveries made by Nilabh Shastri and colleagues that includes the characterisation of cryptic MHC-I peptide antigen epitopes derived from untranslated regions and the N-terminal trimming of peptide antigen precursors by the aminopeptidase ERAAP (ERAP1/2 / ARTS1/LRAP) in the endoplasmic reticulum (ER) prior to the complete assembly of MHC-I complexes and their subsequent exposure to the cell surface. These scientific findings have important implications for developing novel therapeutic approaches in immunotherapy and modern vaccine design.

Original publication

DOI

10.1016/j.cellimm.2022.104638

Type

Journal article

Journal

Cell Immunol

Publication Date

12/2022

Volume

382

Keywords

Adaptive immunity, Antigen, Cryptic epitope, ERAAP, MHC, Major histocompatibility complex, Peptide, Protease, Antigen Presentation, Histocompatibility Antigens Class I, Peptides, Major Histocompatibility Complex, Vaccines