Published in

Rockefeller University Press, Journal of Experimental Medicine, 3(203), p. 647-659, 2006

DOI: 10.1084/jem.20052271

Rockefeller University Press, Journal of Cell Biology, 6(172), p. i14-i14, 2006

DOI: 10.1083/jcb1726oia14

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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

Journal article published in 2006 by Jingbo Yan, Vrajesh V. Parekh, Yanice Mendez-Fernandez, Danyvid Olivares-Villagómez, Srdjan Dragovic, Timothy Hill, Derry C. Roopenian, Sebastian Joyce ORCID, Luc Van Kaer
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

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.