rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
3
|
pubmed:dateCreated |
1990-9-27
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pubmed:abstractText |
The physical association of 40 antigenic peptides and purified HLA class I and class II molecules was monitored using a direct peptide binding assay (PBA) in solid phase and an inhibition peptide binding assay (IPBA) in which the competing peptide was present in a soluble phase. We also examined the ability of different peptides to inhibit the lytic activity of human antiviral cytolytic T cells towards cells incubated with the corresponding target peptide. Our results showed that: (a) Binding of a given human T cell-recognized peptide to several HLA class I and class II molecules occurred frequently. Nevertheless, preferential binding of peptides to their respective restriction molecules was also observed. (b) Binding of HLA molecules to peptides recognized by murine T cells occurred less frequently. (c) 11 of 24 (46%) randomly selected HIV-1 peptides contained agretopic residues allowing their binding to HLA molecules. (d) The kinetics of HLA/peptide association depended on the peptide tested and were faster than or similar to those reported for Ia molecules. Dissociation of these complexes was very low. (e) Peptide/HLA molecule binding was dependent on length, number of positive charges, and presence of hydrophobic residue in the peptide. (f) A correlation was demonstrated between a peptide inhibitory effect in the IPBA and its blocking effect in the cytolytic test. Our data indicated that the restriction phenomenon observed in T cell responses was not strictly related to either an elective HLA/peptide association, or a high binding capacity of a peptide to HLA molecules. These data also showed that the PBA and IPBA are appropriate for the detection of agretopic residues within HIV-1 proteins.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2388036-2409149,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2388036-2413457,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/2388036-2455012,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/2388036-2461519,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/2388036-7035415
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
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pubmed:month |
Sep
|
pubmed:issn |
0022-1007
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
1
|
pubmed:volume |
172
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
889-99
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2388036-Amino Acid Sequence,
pubmed-meshheading:2388036-Antibody Specificity,
pubmed-meshheading:2388036-Antigen-Antibody Complex,
pubmed-meshheading:2388036-Antigens, Viral,
pubmed-meshheading:2388036-HIV-1,
pubmed-meshheading:2388036-HLA Antigens,
pubmed-meshheading:2388036-Histocompatibility Antigens Class I,
pubmed-meshheading:2388036-Histocompatibility Antigens Class II,
pubmed-meshheading:2388036-Humans,
pubmed-meshheading:2388036-Molecular Sequence Data,
pubmed-meshheading:2388036-Peptides,
pubmed-meshheading:2388036-T-Lymphocytes, Cytotoxic,
pubmed-meshheading:2388036-Viral Proteins
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pubmed:year |
1990
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pubmed:articleTitle |
Analysis of physical interactions between peptides and HLA molecules and application to the detection of human immunodeficiency virus 1 antigenic peptides.
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pubmed:affiliation |
Institut National de la Santé et de la Recherche Médicale U152, Hôpital Cochin, Paris, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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