Comparative quantitative mass spectrometry analysis of MHC class II-associated peptides reveals a role of GILT in formation of self-peptide repertoire.

Gamma interferon Inducible Lysosomal Thiol reductase (GILT) is a unique lysosomal reductase that reduces disulfide bonds of endocytosed proteins. Lack of GILT clearly decreases CD4 T cell-antigen specific responses against some epitopes of antigens containing disulfide bonds, but not to proteins wit...

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Autores principales:	Branka Bogunovic, Priya Srinivasan, Yumi Ueda, York Tomita, Maja Maric
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2010
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/c164194e308342d081c28fcdd83ec8ce
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spelling	oai:doaj.org-article:c164194e308342d081c28fcdd83ec8ce2021-12-02T20:21:43ZComparative quantitative mass spectrometry analysis of MHC class II-associated peptides reveals a role of GILT in formation of self-peptide repertoire.1932-620310.1371/journal.pone.0010599https://doaj.org/article/c164194e308342d081c28fcdd83ec8ce2010-05-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20485683/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Gamma interferon Inducible Lysosomal Thiol reductase (GILT) is a unique lysosomal reductase that reduces disulfide bonds of endocytosed proteins. Lack of GILT clearly decreases CD4 T cell-antigen specific responses against some epitopes of antigens containing disulfide bonds, but not to proteins with few or no disulfide bridges. Hence, global impact of GILT on antigen presentation is currently not well understood. We used Nano-LC-ESI-MS/MS to investigate how GILT affects diversity of self-peptides presented by MHC class II molecules. Surprisingly, the repertoire of self-peptides in the absence of GILT does not appear to be significantly different, as only few peptide species (approximately 2%) were found to be the unique indicators of GILT's presence or absence. In the absence of GILT about thirty peptide species (approximately 5%) were found either uniquely or fourteen to hundred fold more abundantly expressed than in the presence of GILT. Our data indicate that GILT has limited yet unexpected effect on self-peptide species presented by MHC class II antigens.Branka BogunovicPriya SrinivasanYumi UedaYork TomitaMaja MaricPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 5, Iss 5, p e10599 (2010)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Branka Bogunovic Priya Srinivasan Yumi Ueda York Tomita Maja Maric Comparative quantitative mass spectrometry analysis of MHC class II-associated peptides reveals a role of GILT in formation of self-peptide repertoire.
description	Gamma interferon Inducible Lysosomal Thiol reductase (GILT) is a unique lysosomal reductase that reduces disulfide bonds of endocytosed proteins. Lack of GILT clearly decreases CD4 T cell-antigen specific responses against some epitopes of antigens containing disulfide bonds, but not to proteins with few or no disulfide bridges. Hence, global impact of GILT on antigen presentation is currently not well understood. We used Nano-LC-ESI-MS/MS to investigate how GILT affects diversity of self-peptides presented by MHC class II molecules. Surprisingly, the repertoire of self-peptides in the absence of GILT does not appear to be significantly different, as only few peptide species (approximately 2%) were found to be the unique indicators of GILT's presence or absence. In the absence of GILT about thirty peptide species (approximately 5%) were found either uniquely or fourteen to hundred fold more abundantly expressed than in the presence of GILT. Our data indicate that GILT has limited yet unexpected effect on self-peptide species presented by MHC class II antigens.
format	article
author	Branka Bogunovic Priya Srinivasan Yumi Ueda York Tomita Maja Maric
author_facet	Branka Bogunovic Priya Srinivasan Yumi Ueda York Tomita Maja Maric
author_sort	Branka Bogunovic
title	Comparative quantitative mass spectrometry analysis of MHC class II-associated peptides reveals a role of GILT in formation of self-peptide repertoire.
title_short	Comparative quantitative mass spectrometry analysis of MHC class II-associated peptides reveals a role of GILT in formation of self-peptide repertoire.
title_full	Comparative quantitative mass spectrometry analysis of MHC class II-associated peptides reveals a role of GILT in formation of self-peptide repertoire.
title_fullStr	Comparative quantitative mass spectrometry analysis of MHC class II-associated peptides reveals a role of GILT in formation of self-peptide repertoire.
title_full_unstemmed	Comparative quantitative mass spectrometry analysis of MHC class II-associated peptides reveals a role of GILT in formation of self-peptide repertoire.
title_sort	comparative quantitative mass spectrometry analysis of mhc class ii-associated peptides reveals a role of gilt in formation of self-peptide repertoire.
publisher	Public Library of Science (PLoS)
publishDate	2010
url	https://doaj.org/article/c164194e308342d081c28fcdd83ec8ce
work_keys_str_mv	AT brankabogunovic comparativequantitativemassspectrometryanalysisofmhcclassiiassociatedpeptidesrevealsaroleofgiltinformationofselfpeptiderepertoire AT priyasrinivasan comparativequantitativemassspectrometryanalysisofmhcclassiiassociatedpeptidesrevealsaroleofgiltinformationofselfpeptiderepertoire AT yumiueda comparativequantitativemassspectrometryanalysisofmhcclassiiassociatedpeptidesrevealsaroleofgiltinformationofselfpeptiderepertoire AT yorktomita comparativequantitativemassspectrometryanalysisofmhcclassiiassociatedpeptidesrevealsaroleofgiltinformationofselfpeptiderepertoire AT majamaric comparativequantitativemassspectrometryanalysisofmhcclassiiassociatedpeptidesrevealsaroleofgiltinformationofselfpeptiderepertoire
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Comparative quantitative mass spectrometry analysis of MHC class II-associated peptides reveals a role of GILT in formation of self-peptide repertoire.

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