Complexes of HLA-G protein on the cell surface are important for leukocyte Ig-like receptor-1 function

J Immunol. 2003 Aug 1;171(3):1343-51. doi: 10.4049/jimmunol.171.3.1343.

Abstract

The nonclassical class I MHC molecule HLA-G is selectively expressed on extravillous cytotrophoblast cells at the maternal-fetal interface during pregnancy. HLA-G can inhibit the killing mediated by NK cells via interaction with the inhibitory NK cell receptor, leukocyte Ig-like receptor-1 (LIR-1). Comparison of the sequence of the HLA-G molecule to other class I MHC proteins revealed two unique cysteine residues located in positions 42 and 147. Mutating these cysteine residues resulted in a dramatic decrease in LIR-1 Ig binding. Accordingly, the mutated HLA-G transfectants were less effective in the inhibition of NK killing and RBL/LIR-1 induced serotonin release. Immunoprecipitation experiments demonstrated the involvement of the cysteine residues in the formation of HLA-G protein oligomers on the cell surface. The cysteine residue located at position 42 is shown to be critical for the expression of such complexes. These oligomers, unique among the class I MHC proteins, probably bind to LIR-1 with increased avidity, resulting in an enhanced inhibitory function of LIR-1 and an impaired killing function of NK cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antigens, CD / metabolism
  • Antigens, CD / physiology*
  • Binding, Competitive / genetics
  • Binding, Competitive / immunology
  • Cell Line, Transformed
  • Cysteine / genetics
  • Cysteine / physiology
  • Cytotoxicity, Immunologic / genetics
  • Decidua / cytology
  • Decidua / immunology
  • Down-Regulation / genetics
  • Down-Regulation / immunology
  • Female
  • HLA Antigens / biosynthesis
  • HLA Antigens / genetics
  • HLA Antigens / metabolism
  • HLA Antigens / physiology*
  • HLA-G Antigens
  • Histocompatibility Antigens Class I / biosynthesis
  • Histocompatibility Antigens Class I / genetics
  • Histocompatibility Antigens Class I / metabolism
  • Histocompatibility Antigens Class I / physiology*
  • Humans
  • Leukocyte Immunoglobulin-like Receptor B1
  • Macromolecular Substances
  • Membrane Glycoproteins / biosynthesis
  • Membrane Glycoproteins / genetics
  • Membrane Glycoproteins / metabolism
  • Membrane Glycoproteins / physiology*
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Protein Binding / genetics
  • Protein Binding / immunology
  • Rats
  • Receptors, Immunologic / antagonists & inhibitors
  • Receptors, Immunologic / metabolism
  • Receptors, Immunologic / physiology*
  • Transfection
  • Tumor Cells, Cultured

Substances

  • Antigens, CD
  • HLA Antigens
  • HLA-G Antigens
  • Histocompatibility Antigens Class I
  • LILRB1 protein, human
  • Leukocyte Immunoglobulin-like Receptor B1
  • Macromolecular Substances
  • Membrane Glycoproteins
  • Receptors, Immunologic
  • Cysteine