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

Jingbo Yan | Vrajesh V Parekh | Yanice Mendez-Fernandez | Danyvid Olivares-Villagómez | Srdjan Dragovic | Timothy Hill | Derry C Roopenian | Sebastian Joyce | Luc Van Kaer
The Journal of experimental medicine | 2006

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.

Pubmed ID: 16505142

Research resources used in this publication

None found

Antibodies used in this publication

None found

Associated grants

  • Agency: NIAID NIH HHS, United States
    Id: R01 AI028802
  • Agency: NHLBI NIH HHS, United States
    Id: P01 HL068744
  • Agency: NIAID NIH HHS, United States
    Id: AI28802
  • Agency: NHLBI NIH HHS, United States
    Id: R01 HL054977
  • Agency: NHLBI NIH HHS, United States
    Id: HL054977
  • Agency: NHLBI NIH HHS, United States
    Id: HL68744

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