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rdf:type |
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lifeskim:mentions |
umls-concept:C0039194,
umls-concept:C0085358,
umls-concept:C0208355,
umls-concept:C0348011,
umls-concept:C1257985,
umls-concept:C1332717,
umls-concept:C1413244,
umls-concept:C1705822,
umls-concept:C1706438,
umls-concept:C1710236,
umls-concept:C2698600
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pubmed:issue |
5675
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pubmed:dateCreated |
2004-5-28
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pubmed:abstractText |
"Cross-priming" describes the activation of naïve CD8+ T cells by professional antigen-presenting cells that have acquired viral or tumor antigens from "donor" cells. Antigen transfer is believed to be mediated by donor cell-derived molecular chaperones bearing short peptide ligands generated by proteasome degradation of protein antigens. We show here that cross-priming is based on the transfer of proteasome substrates rather than peptides. These findings are potentially important for the rational design of vaccines that elicit CD8+ T cell responses.
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pubmed:grant |
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pubmed:commentsCorrections |
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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/Acetylcysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Proteinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Ovalbumin,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Vaccines,
http://linkedlifedata.com/resource/pubmed/chemical/lactacystin
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
28
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pubmed:volume |
304
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1318-21
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15166379-Acetylcysteine,
pubmed-meshheading:15166379-Animals,
pubmed-meshheading:15166379-Antigen Presentation,
pubmed-meshheading:15166379-Antigens,
pubmed-meshheading:15166379-Antigens, Viral,
pubmed-meshheading:15166379-CD8-Positive T-Lymphocytes,
pubmed-meshheading:15166379-Cell Line,
pubmed-meshheading:15166379-Cross-Priming,
pubmed-meshheading:15166379-Cysteine Endopeptidases,
pubmed-meshheading:15166379-Cysteine Proteinase Inhibitors,
pubmed-meshheading:15166379-Endoplasmic Reticulum,
pubmed-meshheading:15166379-Humans,
pubmed-meshheading:15166379-Immunization,
pubmed-meshheading:15166379-Influenza A virus,
pubmed-meshheading:15166379-Lymphocyte Activation,
pubmed-meshheading:15166379-Mice,
pubmed-meshheading:15166379-Mice, Inbred C57BL,
pubmed-meshheading:15166379-Mice, Transgenic,
pubmed-meshheading:15166379-Molecular Chaperones,
pubmed-meshheading:15166379-Multienzyme Complexes,
pubmed-meshheading:15166379-Ovalbumin,
pubmed-meshheading:15166379-Peptide Fragments,
pubmed-meshheading:15166379-Proteasome Endopeptidase Complex,
pubmed-meshheading:15166379-Recombinant Fusion Proteins,
pubmed-meshheading:15166379-Vaccines,
pubmed-meshheading:15166379-Vaccinia virus
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pubmed:year |
2004
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pubmed:articleTitle |
CD8+ T cell cross-priming via transfer of proteasome substrates.
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pubmed:affiliation |
Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda MD, 20892-0440, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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