pubmed-article:2388036 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2388036 | lifeskim:mentions | umls-concept:C0019704 | lld:lifeskim |
pubmed-article:2388036 | lifeskim:mentions | umls-concept:C0567416 | lld:lifeskim |
pubmed-article:2388036 | lifeskim:mentions | umls-concept:C0019721 | lld:lifeskim |
pubmed-article:2388036 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
pubmed-article:2388036 | lifeskim:mentions | umls-concept:C1511790 | lld:lifeskim |
pubmed-article:2388036 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:2388036 | lifeskim:mentions | umls-concept:C0185125 | lld:lifeskim |
pubmed-article:2388036 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:2388036 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:2388036 | pubmed:dateCreated | 1990-9-27 | lld:pubmed |
pubmed-article:2388036 | 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. | lld:pubmed |
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pubmed-article:2388036 | pubmed:language | eng | lld:pubmed |
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pubmed-article:2388036 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:2388036 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2388036 | pubmed:month | Sep | lld:pubmed |
pubmed-article:2388036 | pubmed:issn | 0022-1007 | lld:pubmed |
pubmed-article:2388036 | pubmed:author | pubmed-author:GomardEE | lld:pubmed |
pubmed-article:2388036 | pubmed:author | pubmed-author:ChoppinJJ | lld:pubmed |
pubmed-article:2388036 | pubmed:author | pubmed-author:LévyJ PJP | lld:pubmed |
pubmed-article:2388036 | pubmed:author | pubmed-author:MartinonFF | lld:pubmed |
pubmed-article:2388036 | pubmed:author | pubmed-author:BouillotMM | lld:pubmed |
pubmed-article:2388036 | pubmed:author | pubmed-author:BahraouiEE | lld:pubmed |
pubmed-article:2388036 | pubmed:author | pubmed-author:ConnanFF | lld:pubmed |
pubmed-article:2388036 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2388036 | pubmed:day | 1 | lld:pubmed |
pubmed-article:2388036 | pubmed:volume | 172 | lld:pubmed |
pubmed-article:2388036 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2388036 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2388036 | pubmed:pagination | 889-99 | lld:pubmed |
pubmed-article:2388036 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:2388036 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:2388036 | pubmed:articleTitle | Analysis of physical interactions between peptides and HLA molecules and application to the detection of human immunodeficiency virus 1 antigenic peptides. | lld:pubmed |
pubmed-article:2388036 | pubmed:affiliation | Institut National de la Santé et de la Recherche Médicale U152, Hôpital Cochin, Paris, France. | lld:pubmed |
pubmed-article:2388036 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2388036 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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