Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
16
|
| pubmed:dateCreated |
1994-12-19
|
| pubmed:abstractText |
The adenovirus early region 3 glycoprotein E3-19k binds to and inhibits expression of class I major histocompatibility complex (MHC)-encoded molecules, which may help infected cells evade immune recognition. The role of specific regions of the class I MHC molecule in the interaction with E3-19k was evaluated using a series of HLA-A2.1-, HLA-A2 variant-, and HLA-B7-expressing cell lines. The monoclonal antibody (mAb) W6/32, which recognizes a monomorphic epitope on class I MHC molecules, readily co-immunoprecipitated E3-19k with HLA-A2.1 and 14 different HLA-A2 variant molecules that differ from HLA-A2.1 by single amino acid substitutions. Thus, no single residue tested in the regions of the class I MHC molecule that bind peptide or the T-cell receptor controls the binding to E3-19k. Additional immunoprecipitations performed with mAbs directed against well-defined epitopes on the surface of HLA-A2.1 revealed a dichotomy in the ability of the mAbs to co-immunoprecipitate HLA-A2.1 and E3-19k. The mAbs LGIII-220 (directed against the C-terminal end of the alpha 1-helix), CR11-351 (directed against the N-terminal end of the alpha 2-helix), and PA2.1 (directed against the middle of the alpha 2-helix and an underlying beta-loop) readily co-precipitated HLA-A2.1 and E3-19k. In contrast, mAbs MA2.1 (directed against the N-terminal end of the alpha 1-helix and the C-terminal end of the alpha 2-helix) and HO-2 (directed against the N-terminal end of the alpha 1-helix) did not co-precipitate E3-19k with HLA-A2.1. Similarly, mAb MB40.2 (directed against residues 169-182 of HLA-B7) also did not co-precipitate E3-19k with HLA-B7. These studies lead to the conclusion that the N-terminal end of the alpha 1-helix and the C-terminal end of the alpha 2-helix play an important role in dictating the ability of the E3-19k protein to bind to the class I MHC molecule.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0161-5890
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
31
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1277-84
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:7969188-Adenovirus E3 Proteins,
pubmed-meshheading:7969188-Adenoviruses, Human,
pubmed-meshheading:7969188-Amino Acid Sequence,
pubmed-meshheading:7969188-Antibodies, Monoclonal,
pubmed-meshheading:7969188-Binding Sites,
pubmed-meshheading:7969188-Cell Line,
pubmed-meshheading:7969188-HLA-A2 Antigen,
pubmed-meshheading:7969188-HLA-B7 Antigen,
pubmed-meshheading:7969188-Humans,
pubmed-meshheading:7969188-Molecular Sequence Data,
pubmed-meshheading:7969188-Mutagenesis, Site-Directed,
pubmed-meshheading:7969188-Radioimmunoprecipitation Assay,
pubmed-meshheading:7969188-Structure-Activity Relationship
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
Identification of class I MHC regions which bind to the adenovirus E3-19k protein.
|
| pubmed:affiliation |
Department of Medicine, Medical College of Wisconsin, Milwaukee.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|