title: Coping with loss of perfection in the MHC class I peptide repertoire.
abstract: The MHC class I molecules present thousands of peptides (pMHC I) on the cell surface for immune surveillance by CD8 T cells. The pMHC I repertoire normally contains peptides of perfect length and sequences suitable for binding each MHC I. The peptides are made by first fragmenting cytoplasmic proteins. The fragments are then transported into the endoplasmic reticulum (ER), where they are trimmed to appropriate length by the ER aminopeptidase associated with antigen processing (ERAAP) to generate the final pMHC I. Here, we review studies on the role of ERAAP in generating pMHC I from endogenous or viral proteins and their ability to elicit CD8 T cell responses. The absence of ERAAP profoundly disrupts the pMHC I repertoire which can have major consequences on the immune responses to endogenous and viral antigens.
authors.affiliation: Division of Immunology, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720-3200, USA.
authors.forename: Nicolas
authors.initials: N
authors.lastname: Blanchard
authors.forename: Nilabh
authors.initials: N
authors.lastname: Shastri
mesh_terms: D000818:Animals; D017951:Antigen Presentation; D015395:Histocompatibility Antigens Class I / Q000378:metabolism*; D006801:Humans; D007931:Leucyl Aminopeptidase / Q000378:metabolism; D051379:Mice; D010455:Peptides / Q000737:chemistry / Q000276:immunology* / Q000378:metabolism; D014764:Viral Proteins / Q000276:immunology
chemical_list: D015395:Histocompatibility Antigens Class I; D010455:Peptides; D014764:Viral Proteins; D007931:Leucyl Aminopeptidase; C456799:puromycin-insensitive leucyl-specific aminopeptidase