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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2002-3-7
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pubmed:abstractText |
Immunodominant T cell epitopes from the autoantigen human cartilage glycoprotein 39 have previously been mapped in the context of HLA-DR*0401 and *0402, using mice expressing HLA-DR4 transgenes. We measured the dissociation rates of these epitopes from soluble recombinant DR*0401 and DR*0402 to assess the relationship between peptide/HLA-DR4 kinetic stability and immunogenicity. Experiments were performed at endosomal pH (5.5) and at cell surface pH (7), in the absence and presence of soluble recombinant HLA-DM (sDM). All (4/4) immunodominant peptide/HLA-DR complexes exhibit dissociation half-times of 1h to several days. In contrast, most (3/4) non-immunodominant complexes dissociate with half-times <30 min under at least one of these conditions. Interestingly, a complex which is stable except in the presence of HLA-DM at pH 5.5 is immunogenic only following peptide immunization, while a complex which is stable at acidic but not at neutral pH, is non-immunogenic following either whole protein or peptide immunization. These data indicate that kinetic stability of peptide/MHC complexes in vivo is a key determinant of immunogenicity.
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pubmed:grant |
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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/Adipokines,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/CHI3L1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-D Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-DM antigens,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-DR4 Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Immunodominant Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0014-2980
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pubmed:author |
pubmed-author:BelmaresMichaelM,
pubmed-author:BuschRobertR,
pubmed-author:CopeAndrew PAP,
pubmed-author:HallFrances CFC,
pubmed-author:McConnellHarden MHM,
pubmed-author:MellinsElizabeth DED,
pubmed-author:PatelSalilS,
pubmed-author:PatilNamrata SNS,
pubmed-author:RabinowitzJoshua DJD,
pubmed-author:SonderstrupGreteG,
pubmed-author:ViscontiKevin CKC
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pubmed:issnType |
Print
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pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
662-70
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:11857340-Adipokines,
pubmed-meshheading:11857340-Amino Acid Sequence,
pubmed-meshheading:11857340-Animals,
pubmed-meshheading:11857340-Antigen Presentation,
pubmed-meshheading:11857340-Antigens,
pubmed-meshheading:11857340-Cell Membrane,
pubmed-meshheading:11857340-Cells, Cultured,
pubmed-meshheading:11857340-DNA, Complementary,
pubmed-meshheading:11857340-Drosophila melanogaster,
pubmed-meshheading:11857340-Endosomes,
pubmed-meshheading:11857340-Glycoproteins,
pubmed-meshheading:11857340-HLA-D Antigens,
pubmed-meshheading:11857340-HLA-DR4 Antigen,
pubmed-meshheading:11857340-Humans,
pubmed-meshheading:11857340-Hybridomas,
pubmed-meshheading:11857340-Hydrogen-Ion Concentration,
pubmed-meshheading:11857340-Immunization,
pubmed-meshheading:11857340-Immunodominant Epitopes,
pubmed-meshheading:11857340-Kinetics,
pubmed-meshheading:11857340-Lectins,
pubmed-meshheading:11857340-Macromolecular Substances,
pubmed-meshheading:11857340-Mice,
pubmed-meshheading:11857340-Mice, Transgenic,
pubmed-meshheading:11857340-Molecular Sequence Data,
pubmed-meshheading:11857340-Peptide Fragments,
pubmed-meshheading:11857340-Recombinant Fusion Proteins,
pubmed-meshheading:11857340-Structure-Activity Relationship,
pubmed-meshheading:11857340-T-Lymphocytes
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pubmed:year |
2002
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pubmed:articleTitle |
Relationship between kinetic stability and immunogenicity of HLA-DR4/peptide complexes.
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pubmed:affiliation |
Department of Microbiology and Immunology, Stanford University, Stanford, CA 94305, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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