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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
1990-6-6
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pubmed:abstractText |
T-cell recognition of peptides that are bound and presented by class I major histocompatibility complex molecules is highly specific. At present it is unclear what role class I peptide binding plays relative to T-cell receptor specificity in determination of immune recognition. A previous study from our group demonstrated that the HLA-A2.1 molecule could bind to 25% of the members of a panel of unrelated synthetic peptides as assessed by a functional peptide competition assay. To determine the peptide-binding specificity of another HLA class I molecule, we have examined the capacity of this panel of peptides to compete for the presentation of influenza virus nucleoprotein peptide NP-(335-350) by HLA-B37 to NP-peptide-specific HLA-B37-restricted cytotoxic T-lymphocyte lines. Forty-two percent of peptides tested were capable of inhibiting NP-(335-350) presentation by HLA-B37. Remarkably, none of these HLA-B37-binding peptides belong to the subset that was previously shown to bind to the HLA-A2.1 molecule. Only the NP-(335-350) peptide was capable of binding to both HLA-A2.1 and HLA-B37. These findings demonstrate that the peptide-binding specificities of HLA-B37 and HLA-A2.1 are largely nonoverlapping and suggest that, from the universe of peptides, individual HLA class I molecules can bind to clearly distinct subsets of these peptides.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-1690682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-2320591,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-2430041,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-2433769,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-2438367,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-2443855,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-2459213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-2461564,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-2472444,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-2473117,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-2480387,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-2535860,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-2553813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-2594067,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-2666863,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-2715640,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-2717617,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-2786149,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-2786997,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-2918908,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-2942939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-2982951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-3261776,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-3309677,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-3459185,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-3487084,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-3536303,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-3876513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-6153199,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-6278729,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2333291-6583704
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
87
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3420-4
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:2333291-Adult,
pubmed-meshheading:2333291-Amino Acid Sequence,
pubmed-meshheading:2333291-Binding, Competitive,
pubmed-meshheading:2333291-Cells, Cultured,
pubmed-meshheading:2333291-HLA-A2 Antigen,
pubmed-meshheading:2333291-HLA-B Antigens,
pubmed-meshheading:2333291-HLA-B37 Antigen,
pubmed-meshheading:2333291-Humans,
pubmed-meshheading:2333291-Kinetics,
pubmed-meshheading:2333291-Molecular Sequence Data,
pubmed-meshheading:2333291-Peptides,
pubmed-meshheading:2333291-Protein Binding,
pubmed-meshheading:2333291-Structure-Activity Relationship,
pubmed-meshheading:2333291-T-Lymphocytes,
pubmed-meshheading:2333291-T-Lymphocytes, Cytotoxic
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pubmed:year |
1990
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pubmed:articleTitle |
HLA-B37 and HLA-A2.1 molecules bind largely nonoverlapping sets of peptides.
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pubmed:affiliation |
Molecular Immunology Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892.
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pubmed:publicationType |
Journal Article
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