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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1987-11-12
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pubmed:abstractText |
We previously described a somatic cell expressing a variant H-2Dd molecule that did not serve as a target for alloreactive anti-Dd CTL. The mutant cell line had been isolated by its failure to express a serological epitope present on the H-2Dd alpha 3 domain. In the present study the alpha 3 domain of the Dd molecule of this somatic cell variant was sequenced and a single nucleotide change resulting in a glutamic acid to lysine substitution at residue 227 was identified. This change was reproduced in the cloned H-2Dd gene by oligonucleotide-directed mutagenesis. Cells transfected with this mutant gene were not killed by anti-H-2Dd CTL. Because previous studies using hybrid H-2 class I molecules had established that the alpha 3 domain does not express allele-specific determinants recognized by CTL, our results raise the possibility that residues in the alpha 3 domain of H-2 class I molecules are critical for CTL recognition and constitute a conserved (or monomorphic) determinant recognized by CTL.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-11894934,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-11894963,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-2419473,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-2431046,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-3023861,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-3031507,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-3305739,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-3722821,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-3856254,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-3887412,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-3925069,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-3964822,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-4504350,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-518835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-6088078,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-6096831,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-6184620,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-6188160,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-6189891,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-6194241,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-6201750,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-6205070,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-6226585,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-6302702,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-6315713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-6399975,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-6413636,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-6438633,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-6604749,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-6952248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-6975943,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-7118211,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3498790-7333655
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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 |
Oct
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pubmed:issn |
0022-1007
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
166
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
956-66
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:3498790-Amino Acids,
pubmed-meshheading:3498790-Animals,
pubmed-meshheading:3498790-Cell Line,
pubmed-meshheading:3498790-DNA,
pubmed-meshheading:3498790-H-2 Antigens,
pubmed-meshheading:3498790-Interleukin-2,
pubmed-meshheading:3498790-Mice,
pubmed-meshheading:3498790-Mutation,
pubmed-meshheading:3498790-Structure-Activity Relationship,
pubmed-meshheading:3498790-T-Lymphocytes, Cytotoxic,
pubmed-meshheading:3498790-Transfection
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pubmed:year |
1987
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pubmed:articleTitle |
A single amino acid substitution in the alpha 3 domain of an H-2 class I molecule abrogates reactivity with CTL.
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pubmed:affiliation |
Department of Pathology, Albert Einstein College of Medicine, New York 10461.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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