4.8 Article

ERAAP synergizes with MHC class I molecules to make the final cut in the antigenic peptide precursors in the endoplasmic reticulum

期刊

IMMUNITY
卷 25, 期 5, 页码 795-806

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CELL PRESS
DOI: 10.1016/j.immuni.2006.09.012

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  1. NIAID NIH HHS [R01 AI060040, R01 AI039548, R01 AI039548-11, R01 AI060040-04, R37 AI060040, R01 AI039548-12, R01 AI060040-05] Funding Source: Medline

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The major histocompatibility complex class 1 molecules display peptides (pMHC 1) on the cell surface for immune surveillance by CD8(+) T cells. These peptides are generated by proteolysis of intracellular polypeptides by the proteasome in the cytoplasm and then in the endoplasmic reticulum (ER) by the ER aminopeptidase associated with antigen processing (ERAAP). To define the unknown mechanism of ERAAP function in vivo, we analyzed naturally processed peptides in cells with or without appropriate MHC 1 and ERAAP. In the absence of MHC 1, ERAAP degraded the antigenic precursors in the ER. However, MHC 1 molecules could bind proteolytic intermediates and were essential for generation of the final peptide by ERAAP. Thus, ERAAP synergizes with MHC 1 to generate the final pMHC 1 repertoire.

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