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Altered structure of HLA class I heavy chains associated with mouse beta-2 microglobulin
- Source :
- Immunogenetics. 21:321-331
- Publication Year :
- 1985
- Publisher :
- Springer Science and Business Media LLC, 1985.
-
Abstract
- The serological reactivities of HLA-A3, -B7, and -CW3 heavy chains associated with either mouse, bovine, or human beta-2-microglobulin (beta 2m) and expressed on the surface of transfected mouse fibroblasts were analyzed. All reactivities associated with one cluster (defined by monoclonal antibody W6/32) of antigenic determinants expressed by these HLA class I molecules were lost, or profoundly reduced, after each heavy chain associated with mouse beta 2-m. Expression by the transfected fibroblasts of the HLA-A3, -B7, and -CW3 heavy chains in association with human beta 2m restores these reactivities. Since most of the amino acid differences between mouse and human beta 2m probably correspond to externally oriented hydrophilic residues, these results suggest that critical interactions in the three-dimensional structure of HLA class I molecules occur between the light chain and the first two external domains of the class I heavy chains, to which some of the altered reactivities have been mapped.
- Subjects :
- Ratón
medicine.drug_class
Immunology
Molecular Conformation
Human leukocyte antigen
Biology
Transfection
Monoclonal antibody
Immunoglobulin light chain
Epitopes
Mice
Antigen
HLA Antigens
Genetics
medicine
Animals
Humans
Cloning, Molecular
Cells, Cultured
chemistry.chemical_classification
Binding Sites
Beta-2 microglobulin
Antibodies, Monoclonal
Molecular biology
Amino acid
chemistry
beta 2-Microglobulin
Subjects
Details
- ISSN :
- 14321211 and 00937711
- Volume :
- 21
- Database :
- OpenAIRE
- Journal :
- Immunogenetics
- Accession number :
- edsair.doi.dedup.....a4d611986953513d38eab5b858770169