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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


  • Boyson JE
  • Erskine R
  • Whitman MC
  • Chiu M
  • Lau JM
  • Koopman LA
  • Valter MM
  • Angelisova P
  • Horejsi V
  • Strominger JL


Proceedings of the National Academy of Sciences of the United States of America

Publication Data

December 10, 2002

Associated Grants

  • Agency: NIAID NIH HHS, Id: AI-50207-02
  • Agency: NCI NIH HHS, Id: CA-47554
  • Agency: NICHD NIH HHS, Id: F32 HD008515
  • Agency: NICHD NIH HHS, Id: F32 HD008515-01
  • Agency: NICHD NIH HHS, Id: F32 HD008515-02
  • Agency: NICHD NIH HHS, Id: F32 HD008515-03

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