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rdf:type |
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lifeskim:mentions |
umls-concept:C0003342,
umls-concept:C0018909,
umls-concept:C0019627,
umls-concept:C0039195,
umls-concept:C0040711,
umls-concept:C0205145,
umls-concept:C0205164,
umls-concept:C0217704,
umls-concept:C0332291,
umls-concept:C0449450,
umls-concept:C0456387,
umls-concept:C0524637,
umls-concept:C0733755,
umls-concept:C1514468,
umls-concept:C1721219
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pubmed:issue |
3
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pubmed:dateCreated |
1991-9-26
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pubmed:abstractText |
Class I major histocompatibility complex (MHC) restricted T lymphocytes preferentially recognize fragments of polypeptides processed through a nonendosomal presentation pathway. At present the intracellular compartment(s) in which polypeptide fragmentation occurs and factors which influence the formation of an antigenic epitope are not well understood. To assess the role of residues flanking an antigenic site in the generation of the antigenic moiety recognized by class I MHC restricted T lymphocytes we have moved the coding sequence for an immunodominant H-2Kd restricted site on the influenza A/JAPAN/57 hemagglutinin (residues 202-221) by site-directed mutagenesis to six different positions along the coding sequence of the hemagglutinin gene. We have found that all six classes of mutants are recognized by MHC class I restricted T cells as efficiently as the wild type hemagglutinin gene product. Thus neither N-terminal to C-terminal position within the translation product nor sequences flanking the antigenic site influence processing.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1875170-1700000,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1875170-2196996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1875170-2270487,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1875170-2411422,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1875170-2420472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1875170-2442285,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1875170-2456373,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1875170-2460530,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1875170-2477491,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1875170-2478887,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1875170-2537466,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1875170-3261634,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1875170-3485173,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1875170-3491325,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1875170-6096101,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1875170-6166708
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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 |
Sep
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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 |
174
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
733-6
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:1875170-Amino Acid Sequence,
pubmed-meshheading:1875170-Animals,
pubmed-meshheading:1875170-Antigens, Viral,
pubmed-meshheading:1875170-Base Sequence,
pubmed-meshheading:1875170-DNA Mutational Analysis,
pubmed-meshheading:1875170-H-2 Antigens,
pubmed-meshheading:1875170-Hemagglutinins, Viral,
pubmed-meshheading:1875170-Mice,
pubmed-meshheading:1875170-Molecular Sequence Data,
pubmed-meshheading:1875170-Peptides,
pubmed-meshheading:1875170-Recombinant Proteins,
pubmed-meshheading:1875170-Structure-Activity Relationship,
pubmed-meshheading:1875170-T-Lymphocytes, Cytotoxic
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pubmed:year |
1991
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pubmed:articleTitle |
Presentation of viral antigen to class I major histocompatibility complex-restricted cytotoxic T lymphocyte. Recognition of an immunodominant influenza hemagglutinin site by cytotoxic T lymphocyte is independent of the position of the site in the hemagglutinin translation product.
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pubmed:affiliation |
Department of Pathology, Washington University School of Medicine, St. Louis, Missouri 63110.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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