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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
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 expressi...
Autores principales: | , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2006
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2118255/ https://www.ncbi.nlm.nih.gov/pubmed/16505142 http://dx.doi.org/10.1084/jem.20052271 |
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author | Yan, Jingbo Parekh, Vrajesh V. Mendez-Fernandez, Yanice Olivares-Villagómez, Danyvid Dragovic, Srdjan Hill, Timothy Roopenian, Derry C. Joyce, Sebastian Van Kaer, Luc |
author_facet | Yan, Jingbo Parekh, Vrajesh V. Mendez-Fernandez, Yanice Olivares-Villagómez, Danyvid Dragovic, Srdjan Hill, Timothy Roopenian, Derry C. Joyce, Sebastian Van Kaer, Luc |
author_sort | Yan, Jingbo |
collection | PubMed |
description | 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. |
format | Text |
id | pubmed-2118255 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2006 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21182552007-12-13 In vivo role of ER-associated peptidase activity in tailoring peptides for presentation by MHC class Ia and class Ib molecules Yan, Jingbo Parekh, Vrajesh V. Mendez-Fernandez, Yanice Olivares-Villagómez, Danyvid Dragovic, Srdjan Hill, Timothy Roopenian, Derry C. Joyce, Sebastian Van Kaer, Luc J Exp Med Articles 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. The Rockefeller University Press 2006-03-20 /pmc/articles/PMC2118255/ /pubmed/16505142 http://dx.doi.org/10.1084/jem.20052271 Text en Copyright © 2006, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles Yan, Jingbo Parekh, Vrajesh V. Mendez-Fernandez, Yanice Olivares-Villagómez, Danyvid Dragovic, Srdjan Hill, Timothy Roopenian, Derry C. Joyce, Sebastian Van Kaer, Luc In vivo role of ER-associated peptidase activity in tailoring peptides for presentation by MHC class Ia and class Ib molecules |
title | In vivo role of ER-associated peptidase activity in tailoring peptides for presentation by MHC class Ia and class Ib molecules |
title_full | In vivo role of ER-associated peptidase activity in tailoring peptides for presentation by MHC class Ia and class Ib molecules |
title_fullStr | In vivo role of ER-associated peptidase activity in tailoring peptides for presentation by MHC class Ia and class Ib molecules |
title_full_unstemmed | In vivo role of ER-associated peptidase activity in tailoring peptides for presentation by MHC class Ia and class Ib molecules |
title_short | In vivo role of ER-associated peptidase activity in tailoring peptides for presentation by MHC class Ia and class Ib molecules |
title_sort | in vivo role of er-associated peptidase activity in tailoring peptides for presentation by mhc class ia and class ib molecules |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2118255/ https://www.ncbi.nlm.nih.gov/pubmed/16505142 http://dx.doi.org/10.1084/jem.20052271 |
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