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Disulfide bond-mediated dimerization of HLA-G on the cell surface.

HLA-G is a nonclassical class I MHC molecule with an unknown function and with unusual characteristics that distinguish it from other class I MHC molecules. Here, we demonstrate that HLA-G forms disulfide-linked dimers that are present on the cell surface. Immunoprecipitation of HLA-G from surface biotinylated transfectants using the anti-beta2-microglobulin mAb BBM.1 revealed the presence of an approximately equal 78-kDa form of HLA-G heavy chain that was reduced by using DTT to a 39-kDa form. Mutation of Cys-42 to a serine completely abrogated dimerization of HLA-G, suggesting that the disulfide linkage formed exclusively through this residue. A possible interaction between the HLA-G monomer or dimer and the KIR2DL4 receptor was also investigated, but no interaction between these molecules could be detected through several approaches. The cell-surface expression of dimerized HLA-G molecules may have implications for HLA-Greceptor interactions and for the search for specific receptors that bind HLA-G.

Pubmed ID: 12454284 RIS Download

Mesh terms: Amino Acid Substitution | Antigens, Surface | Choriocarcinoma | Cysteine | Cystine | Dimerization | Dithiothreitol | Female | Genes, MHC Class II | HLA Antigens | HLA-G Antigens | Histocompatibility Antigens Class I | Humans | Molecular Weight | Oxidation-Reduction | Pregnancy | Protein Interaction Mapping | Receptors, Immunologic | Receptors, KIR | Receptors, KIR2DL4 | Recombinant Fusion Proteins | Transfection | Tumor Cells, Cultured | Uterine Neoplasms

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