In vivo role of ER-associated peptidase activity in tailoring peptides for presentation by MHC class Ia and class Ib molecules.

Yan J, Parekh VV, Mendez-Fernandez Y, Olivares-Villagómez D, Dragovic S, Hill T, Roopenian DC, Joyce S, Van Kaer L
J Exp Med. 2006 203 (3): 647-59

PMID: 16505142 · PMCID: PMC2118255 · DOI:10.1084/jem.20052271

Endoplasmic reticulum (ER)-associated aminopeptidase (ERAP)1 has been implicated in the final proteolytic processing of peptides presented by major histocompatibility complex (MHC) class I molecules. To evaluate the in vivo role of ERAP1, we have generated ERAP1-deficient mice. Cell surface expression of the class Ia molecules H-2Kb and H-2Db and of the class Ib molecule Qa-2 was significantly reduced in these animals. Although cells from mutant animals exhibited reduced capacity to present several self- and foreign antigens to Kb-, Db-, or Qa-1b-restricted CD8+ cytotoxic T cells, presentation of some antigens was unaffected or significantly enhanced. Consistent with these findings, mice generated defective CD8+ T cell responses against class I-presented antigens. These findings reveal an important in vivo role of ER-associated peptidase activity in tailoring peptides for presentation by MHC class Ia and class Ib molecules.

MeSH Terms (11)

Aminopeptidases Animals Antigen Presentation CD8-Positive T-Lymphocytes Gene Expression Regulation H-2 Antigens Histocompatibility Antigens Class I Mice Mice, Knockout Minor Histocompatibility Antigens Peptides

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