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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0017355,
umls-concept:C0030956,
umls-concept:C0205409,
umls-concept:C0439851,
umls-concept:C0456387,
umls-concept:C0567416,
umls-concept:C0591833,
umls-concept:C0597551,
umls-concept:C1145667,
umls-concept:C1149098,
umls-concept:C1167622,
umls-concept:C1552596,
umls-concept:C1561491,
umls-concept:C1880022,
umls-concept:C1947931,
umls-concept:C2349209,
umls-concept:C2825311
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pubmed:issue |
7
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pubmed:dateCreated |
1994-10-14
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pubmed:abstractText |
Peptides that are bound by the murine class I MHC molecule H-2Kk have been isolated and sequenced. The initial step in the fractionation was affinity column isolation of the peptide-class I complex from either RDM-4 or x5563 tumor cell lines. Acid denaturation of the complex followed by HPLC fractionation of the peptides allowed us to sequence individual peptides, as well as pools of peptides. To date, a total of 10 sequences have been characterized, and all were 8 mers. The sequences were variable except for glutamic acid in the second position (P2) and isoleucine in the eighth (P8), which were highly conserved. To further study peptide binding to H-2Kk, a competitive binding assay consisting of the immobilized histocompatibility protein and a biotinylated self-peptide for signal generation was developed. A complete set of single-alanine variants for this one self-peptide was tested in the assay, demonstrating that substitution at P2 and P8 markedly decreased the affinity for the class I molecule; alanine at position 3 had an intermediate effect on binding. A comparison of the identified self-peptides for binding to H-2Kk showed that they differed in affinity by more than one order of magnitude. Influenza virus nucleoprotein peptide, SDY EGR LI, associated with the plate-bound class I molecule, and the resulting MHC-peptide complex could trigger TNF release by influenza-primed CTLs. This result demonstrated the functional activity of the plate-bound H-2Kk-peptide complex.
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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/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/H-2 Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0022-1767
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
153
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3079-92
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7522249-Amino Acid Sequence,
pubmed-meshheading:7522249-Animals,
pubmed-meshheading:7522249-Binding, Competitive,
pubmed-meshheading:7522249-Epitopes,
pubmed-meshheading:7522249-H-2 Antigens,
pubmed-meshheading:7522249-Ligands,
pubmed-meshheading:7522249-Mice,
pubmed-meshheading:7522249-Mice, Inbred AKR,
pubmed-meshheading:7522249-Mice, Inbred C3H,
pubmed-meshheading:7522249-Molecular Sequence Data,
pubmed-meshheading:7522249-Nucleoproteins,
pubmed-meshheading:7522249-Orthomyxoviridae,
pubmed-meshheading:7522249-Peptides,
pubmed-meshheading:7522249-Protein Binding,
pubmed-meshheading:7522249-T-Lymphocytes, Cytotoxic,
pubmed-meshheading:7522249-Tumor Necrosis Factor-alpha
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pubmed:year |
1994
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pubmed:articleTitle |
Characterization of peptide binding to the murine MHC class I H-2Kk molecule. Sequencing of the bound peptides and direct binding of synthetic peptides to isolated class I molecules.
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pubmed:affiliation |
Genetics Institute, Inc., Cambridge, MA 02140.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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