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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2005-7-6
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pubmed:abstractText |
It has been shown that exogenous antigens can access the MHC class I pathway of professional antigen-processing cells. However, details as to how the MHC class I-peptide complex forms in the presentation pathway are still poorly understood. Here we used MHC class I-peptide-specific antibodies to investigate the formation and intracellular location of class I-peptide complexes in macrophages. We observed that the formation of class I-peptide complexes occurs within a few hours and lasts for another few hours on the cell surface of macrophages following loading with filamentous phage particles. The class I-peptide complexes in the process were co-localized with MHC class II molecules and endocytic system markers. Moreover, endosomal compartments containing class I-peptide complexes were found within intracellular organelles stained by DiOC6 and calnexin. In addition, the cross-presentation of phage particles was transporter associated with antigen processing (TAP)-dependent and sensitive to proteasome inhibitors and NH(4)Cl. These data suggest that endocytosed phage particles may be processed and cross-presented in organelles positive for phagosome and endoplasmic reticulum (ER) markers via a classical ER MHC class I loading mechanism.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Ammonium Chloride,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Biological Markers,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class I,
http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class II,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/tocopherol-associated protein, mouse
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0014-2980
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
35
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2041-50
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15940671-Ammonium Chloride,
pubmed-meshheading:15940671-Animals,
pubmed-meshheading:15940671-Antigens, Viral,
pubmed-meshheading:15940671-Biological Markers,
pubmed-meshheading:15940671-Carrier Proteins,
pubmed-meshheading:15940671-Cross-Priming,
pubmed-meshheading:15940671-Endoplasmic Reticulum,
pubmed-meshheading:15940671-Histocompatibility Antigens Class I,
pubmed-meshheading:15940671-Histocompatibility Antigens Class II,
pubmed-meshheading:15940671-Hydrogen-Ion Concentration,
pubmed-meshheading:15940671-Inovirus,
pubmed-meshheading:15940671-Kinetics,
pubmed-meshheading:15940671-Lipoproteins,
pubmed-meshheading:15940671-Mice,
pubmed-meshheading:15940671-Mice, Inbred C3H,
pubmed-meshheading:15940671-Mice, Inbred C57BL,
pubmed-meshheading:15940671-Mice, Knockout,
pubmed-meshheading:15940671-Phagocytosis,
pubmed-meshheading:15940671-Proteasome Endopeptidase Complex,
pubmed-meshheading:15940671-Trans-Activators,
pubmed-meshheading:15940671-Transport Vesicles,
pubmed-meshheading:15940671-Virion
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pubmed:year |
2005
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pubmed:articleTitle |
Cross-presentation of phage particle antigen in MHC class II and endoplasmic reticulum marker-positive compartments.
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pubmed:affiliation |
The Institute of Immunology, PLA, The Third Military Medical University, Shapingba District, Chongqing, PR China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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