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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1990-1-5
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pubmed:abstractText |
The expression of transfected HLA class I Ag has previously been shown to protect human target cells from NK-mediated conjugation and cytolysis. In this same system, transfected H-2 class I Ag fail to impart resistance to NK. In this study, we have mapped the portion of the HLA class I molecule involved in this protective effect by exploiting this HLA/H-2 dichotomy. Hybrid class I genes were produced by exon-shuffling between the HLA-B7 and H-2Dp genes, and transfected into the class I Ag-deficient B-lymphoblastoid cell line (B-LCL) C1R. Only those transfectants expressing class I Ag containing the alpha 1 and alpha 2 domains of the HLA molecule are protected from NK, suggesting the "protective epitope" is located within these domains. Since a glycosylation difference exists between HLA and H-2 class I Ag within these domains (i.e., at amino acid residue 176), the role of carbohydrate in the class I protective effect was examined. HLA-B7 mutant genes encoding proteins which either lack the normal carbohydrate addition site at amino acid residue 86 (B7M86-) or possess an additional site at residue 176 (B7M176+) were transfected into C1R. Transfectants expressing either mutant HLA-B7 Ag were protected from NK. Thus, carbohydrate is probably not integral to a class I "protective epitope." The potential for allelic variation in the ability of HLA class I Ag to protect C1R target cells from NK was examined in HLA-A2, A3, B7, and Bw58 transfectants. Although no significant variation exists among the HLA-A3, B7, and Bw58 alleles, HLA-A2 appears unable to protect. Comparison of amino acid sequences suggests a restricted number of residues which may be relevant to the protective effect.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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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 |
143
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3853-7
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:2479694-Amino Acid Sequence,
pubmed-meshheading:2479694-Carbohydrate Conformation,
pubmed-meshheading:2479694-Complement C1r,
pubmed-meshheading:2479694-Cytotoxicity, Immunologic,
pubmed-meshheading:2479694-Epitopes,
pubmed-meshheading:2479694-HLA-A2 Antigen,
pubmed-meshheading:2479694-Histocompatibility Antigens Class I,
pubmed-meshheading:2479694-Humans,
pubmed-meshheading:2479694-Immunity, Innate,
pubmed-meshheading:2479694-Killer Cells, Natural,
pubmed-meshheading:2479694-Male,
pubmed-meshheading:2479694-Molecular Sequence Data,
pubmed-meshheading:2479694-Peptide Mapping
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pubmed:year |
1989
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pubmed:articleTitle |
The alpha 1/alpha 2 domains of class I HLA molecules confer resistance to natural killing.
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pubmed:affiliation |
Department of Microbiology and Immunology, Duke University Medical Center, Durham, NC 27710.
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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.
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