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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
1988-11-3
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pubmed:abstractText |
A large series of HLA-A2/HLA-A3 recombinant genes were generated by using the in vivo recombination technique. These genes have each been modified in the last two-thirds of the third exon such that one or several HLA-A2-specific substitutions have been made in the HLA-A3 gene and vice versa. The recombinant genes were transfected into the murine cell line P815 and the transfectants were used as targets for a series of 20 human CTL lines or clones specific for HLA-A2 or HLA-A3, or restricted by HLA-A2 and specific for influenza A. Several patterns of anti-HLA-A2, anti-HLA-A3, and HLA-A2-restricted anti-influenza CTL activity were observed and when uncloned cell lines were studied, a progressive selection of some clones with a similar pattern of activity was regularly found. From the comparison of these different patterns the following conclusions can be drawn: 1) In most but not all cases both domains of the class I molecule were essential for CTL recognition, but residue 152 was critically important for the majority of CTL tested; 2) amino acids 114/116 were also critical in most cases, and their position close to amino acid 152 in the tertiary structure of the molecule may have some functional significance; and 3) amino acid 161, although highly conserved, plays an unexpected but very important role in CTL function.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antilymphocyte Serum,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-A Antigens,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-A2 Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/HLA-A3 Antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides
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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 |
141
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2487-96
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2459213-Amino Acids,
pubmed-meshheading:2459213-Animals,
pubmed-meshheading:2459213-Antibodies, Monoclonal,
pubmed-meshheading:2459213-Antilymphocyte Serum,
pubmed-meshheading:2459213-Binding, Competitive,
pubmed-meshheading:2459213-Blood Donors,
pubmed-meshheading:2459213-Cell Line,
pubmed-meshheading:2459213-Cytotoxicity Tests, Immunologic,
pubmed-meshheading:2459213-Epitopes,
pubmed-meshheading:2459213-HLA-A Antigens,
pubmed-meshheading:2459213-HLA-A2 Antigen,
pubmed-meshheading:2459213-HLA-A3 Antigen,
pubmed-meshheading:2459213-Humans,
pubmed-meshheading:2459213-Influenza A virus,
pubmed-meshheading:2459213-Mice,
pubmed-meshheading:2459213-Peptides,
pubmed-meshheading:2459213-T-Lymphocytes, Cytotoxic
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pubmed:year |
1988
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pubmed:articleTitle |
A study of functionally active amino acids involved in the interaction of HLA-A2 or HLA-A3 molecules with cytolytic T lymphocytes.
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pubmed:affiliation |
Laboratoire d'Immunologie et de Virologie des Tumeurs, INSERM 152, Paris, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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