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

Author:

Yan Jingbo1,Parekh Vrajesh V.1,Mendez-Fernandez Yanice1,Olivares-Villagómez Danyvid1,Dragovic Srdjan1,Hill Timothy1,Roopenian Derry C.2,Joyce Sebastian1,Van Kaer Luc1

Affiliation:

1. Department of Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, TN 37232

2. The Jackson Laboratory, Bar Harbor, ME 04609

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.

Publisher

Rockefeller University Press

Subject

Immunology,Immunology and Allergy

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