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http://purl.uniprot.org/citations/15723810http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15723810http://www.w3.org/2000/01/rdf-schema#comment"Major Histocompatibility Complex (MHC) class II molecules, including Human Leukocyte Antigen (HLA)-DR, present peptide fragments from proteins degraded in the endocytic pathway. HLA-DR is targeted to late-endocytic structures named MHC class II-containing Compartments (MIIC), where it interacts with HLA-DM. This chaperone stabilizes HLA-DR during peptide exchange and is critical for successful peptide loading. To follow this process in living cells, we have generated cells containing HLA-DR3/Cyan Fluorescent Protein (CFP), HLA-DM/Yellow Fluorescent Protein (YFP), and invariant chain. HLA-DR/DM interactions were observed by Fluorescence Resonance Energy Transfer (FRET). These interactions were pH insensitive, yet occurred only in internal structures and not at the limiting membrane of MIIC. In a cellular model of infection, phagosomes formed a limiting membrane surrounding internalized Salmonella. HLA-DR and HLA-DM did not interact in Salmonella-induced vacuoles, and HLA-DR was not loaded with antigens. The absence of HLA-DR/DM interactions at the limiting membrane prevents local loading of MHC class II molecules in phagosomes. This may allow these bacteria to successfully evade the immune system."xsd:string
http://purl.uniprot.org/citations/15723810http://purl.org/dc/terms/identifier"doi:10.1016/j.immuni.2005.01.006"xsd:string
http://purl.uniprot.org/citations/15723810http://purl.uniprot.org/core/author"Janssen H."xsd:string
http://purl.uniprot.org/citations/15723810http://purl.uniprot.org/core/author"Neefjes J."xsd:string
http://purl.uniprot.org/citations/15723810http://purl.uniprot.org/core/author"Janssen L."xsd:string
http://purl.uniprot.org/citations/15723810http://purl.uniprot.org/core/author"Kuijl C."xsd:string
http://purl.uniprot.org/citations/15723810http://purl.uniprot.org/core/author"van Ham M."xsd:string
http://purl.uniprot.org/citations/15723810http://purl.uniprot.org/core/author"Calafat J."xsd:string
http://purl.uniprot.org/citations/15723810http://purl.uniprot.org/core/author"van Lith M."xsd:string
http://purl.uniprot.org/citations/15723810http://purl.uniprot.org/core/author"Jalink K."xsd:string
http://purl.uniprot.org/citations/15723810http://purl.uniprot.org/core/author"van Rheenen J."xsd:string
http://purl.uniprot.org/citations/15723810http://purl.uniprot.org/core/author"Zwart W."xsd:string
http://purl.uniprot.org/citations/15723810http://purl.uniprot.org/core/author"Marsman M."xsd:string
http://purl.uniprot.org/citations/15723810http://purl.uniprot.org/core/author"Griekspoor A."xsd:string
http://purl.uniprot.org/citations/15723810http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15723810http://purl.uniprot.org/core/name"Immunity"xsd:string
http://purl.uniprot.org/citations/15723810http://purl.uniprot.org/core/pages"221-233"xsd:string
http://purl.uniprot.org/citations/15723810http://purl.uniprot.org/core/title"Spatial separation of HLA-DM/HLA-DR interactions within MIIC and phagosome-induced immune escape."xsd:string
http://purl.uniprot.org/citations/15723810http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/15723810http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15723810
http://purl.uniprot.org/citations/15723810http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15723810
http://purl.uniprot.org/uniprot/#_A0A1V0E3I4-mappedCitation-15723810http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15723810
http://purl.uniprot.org/uniprot/#_A0A1V0E3I5-mappedCitation-15723810http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15723810
http://purl.uniprot.org/uniprot/#_A0A1V0E3J1-mappedCitation-15723810http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15723810