Source:http://linkedlifedata.com/resource/pubmed/id/21788443
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2011-8-22
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pubmed:abstractText |
In APCs, presentation by MHC II molecules of the chemically dominant peptide from the protein hen egg white lysozyme (HEL) generates different conformational isomers of the peptide-MHC II complexes (pMHC). Type B pMHCs are formed in early endosomes from exogenous peptides in the absence of H2-DM, whereas in contrast, type A pMHC complexes are formed from HEL protein in late vesicles after editing by H2-DM. Thus, H2-DM edits off the more unstable pMHC complexes, which are not presented from HEL. In this study, we show that type B pMHC complexes were presented from HEL protein only after stimulation of dendritic cells (DC) with TLR ligands or type I IFN. Type I IFN contributed to most TLR ligand-induced type B pMHC generation, as presentation decreased in DC lacking the receptor for type I IFNs (IFNAR1(-/-)). In contrast, presentation of type A pMHC from HEL and from peptide was minimally affected by TLR ligands. The relative effectiveness of CD8?(+) DC or CD8?(-) DC in presenting type B pMHC complexes varied depending on the TLR ligand used. The mechanisms of generation of type B pMHC from HEL protein with TLR stimulation did not involve H2-DM or release of peptides. DC from H2-DM-deficient mice in the presence of TLR ligands presented type B pMHC. Such DC showed a slight enhancement of HEL catabolism, but peptide release was not evident. Thus, TLR ligands and type I IFN alter the pathways of presentation by MHC II molecules of DC such that type B pMHCs are generated from protein Ag.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class II,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon Type I,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Muramidase,
http://linkedlifedata.com/resource/pubmed/chemical/Toll-Like Receptors,
http://linkedlifedata.com/resource/pubmed/chemical/hen egg lysozyme
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1550-6606
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
187
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2193-201
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pubmed:meshHeading |
pubmed-meshheading:21788443-Animals,
pubmed-meshheading:21788443-Antigen Presentation,
pubmed-meshheading:21788443-Cell Separation,
pubmed-meshheading:21788443-Dendritic Cells,
pubmed-meshheading:21788443-Flow Cytometry,
pubmed-meshheading:21788443-Histocompatibility Antigens Class II,
pubmed-meshheading:21788443-Interferon Type I,
pubmed-meshheading:21788443-Ligands,
pubmed-meshheading:21788443-Major Histocompatibility Complex,
pubmed-meshheading:21788443-Mice,
pubmed-meshheading:21788443-Mice, Knockout,
pubmed-meshheading:21788443-Muramidase,
pubmed-meshheading:21788443-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:21788443-Toll-Like Receptors
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pubmed:year |
2011
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pubmed:articleTitle |
Presentation of type B peptide-MHC complexes from hen egg white lysozyme by TLR ligands and type I IFNs independent of H2-DM regulation.
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pubmed:affiliation |
Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO 63110, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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