期刊
JOURNAL OF EXPERIMENTAL MEDICINE
卷 203, 期 3, 页码 647-659出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1084/jem.20052271
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资金
- NHLBI NIH HHS [HL054977, HL68744, P01 HL068744, R01 HL054977] Funding Source: Medline
- NIAID NIH HHS [AI28802, R01 AI028802] Funding Source: Medline
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-2K(b) and H-2D(b) 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 K-b-, D-b-, or Qa-1(b)-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.
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