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• W1992099618 abstract "The aminopeptidase ERAAP trims peptides loaded onto MHC class I molecules and can be targeted during evasion of the immune response by pathogens. Shastri and colleagues show that inhibition of ERAAP identifies a protective nonclassical MHC presentation pathway involving Qa-1. The aminopeptidase ERAAP is essential for trimming peptides presented by major histocompatibility complex (MHC) class I molecules. Inhibition of ERAAP by cytomegalovirus results in evasion of the immune response by this virus, and polymorphisms in ERAAP are associated with autoimmune disorders. How normal ERAAP function is monitored is unknown. We found that inhibition of ERAAP rapidly induced presentation of the peptide FYAEATPML (FL9) by the MHC class Ib molecule Qa-1b. Antigen-experienced T cells specific for the Qa-1b–FL9 complex were frequent in naive mice. Wild-type mice immunized with ERAAP-deficient cells mounted a potent CD8+ T cell response specific for Qa-1b–FL9. MHC class Ib–restricted cytolytic effector cells specifically eliminated ERAAP-deficient cells in vitro and in vivo. Thus, nonclassical Qa-1b–peptide complexes direct cytotoxic T cells to targets with defective antigen processing in the endoplasmic reticulum." @default.
• W1992099618 created "2016-06-24" @default.
• W1992099618 creator A5063729633 @default.
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• W1992099618 date "2012-04-22" @default.
• W1992099618 modified "2023-10-10" @default.
• W1992099618 title "Nonclassical MHC class Ib–restricted cytotoxic T cells monitor antigen processing in the endoplasmic reticulum" @default.
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• W1992099618 doi "https://doi.org/10.1038/ni.2282" @default.
• W1992099618 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3362685" @default.
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