Erap1 enzyme-Mediated trimming and structural analyses of mhc i-Bound precursor peptides yield novel insights into antigen processing and presentation.
Endoplasmic reticulum aminopeptidase 1 (ERAP1) and ERAP2 critically shape the
major histocompatibility complex I (MHC I) immunopeptidome. The ERAPs remove
N-terminal residues from antigenic precursor peptides and generate
optimal-length peptides (i.e. 8-10-mers) to fit into the MHC class I
groove. It is therefore intriguing that MHC class I molecules can present
N-terminally extended peptides on the cell surface that can elicit CD8+ T-cell
responses. This observation likely reflects gaps in our understanding of how
antigens are processed by the ERAP enzymes. To better understand ERAPs' function
in antigen processing, here we generated a nested set of N-terminally extended
10-20-mer peptides (RA)
