Mutational analysis of the human 2B4 (CD244)/CD48 interaction: Lys68 and Glu70 in the V domain of 2B4 are critical for CD48 binding and functional activation of NK cells

J Immunol. 2005 Jul 15;175(2):1005-13. doi: 10.4049/jimmunol.175.2.1005.

Abstract

Interaction between receptors and ligands plays a critical role in the generation of immune responses. The 2B4 (CD244), a member of the CD2 subset of the Ig superfamily, is the high affinity ligand for CD48. It is expressed on NK cells, T cells, monocytes, and basophils. Recent data indicate that 2B4/CD48 interactions regulate NK and T lymphocyte functions. In human NK cells, 2B4/CD48 interaction induces activation signals, whereas in murine NK cells it sends inhibitory signals. To determine the structural basis for 2B4/CD48 interaction, selected amino acid residues in the V domain of the human 2B4 (h2B4) were mutated to alanine by site-directed mutagenesis. Following transient expression of these mutants in B16F10 melanoma cells, their interaction with soluble CD48-Fc fusion protein was assessed by flow cytometry. We identified amino acid residues in the extracellular domain of h2B4 that are involved in interacting with CD48. Binding of CD48-Fc fusion protein to RNK-16 cells stably transfected with wild-type and a double-mutant Lys(68)Ala-Glu(70)Ala h2B4 further demonstrated that Lys(68) and Glu(70) in the V domain of h2B4 are essential for 2B4/CD48 interaction. Functional analysis indicated that Lys(68) and Glu(70) in the extracellular domain of h2B4 play a key role in the activation of human NK cells through 2B4/CD48 interaction.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alanine / genetics
  • Amino Acid Sequence
  • Animals
  • Antigens, CD / chemistry
  • Antigens, CD / genetics*
  • Antigens, CD / metabolism*
  • Antigens, Surface / chemistry
  • Antigens, Surface / metabolism*
  • Antigens, Surface / physiology
  • CD48 Antigen
  • Cytotoxicity, Immunologic / genetics*
  • DNA Mutational Analysis
  • Dimerization
  • Down-Regulation / genetics
  • Down-Regulation / immunology
  • Glutamic Acid / genetics*
  • Glutamic Acid / metabolism
  • Humans
  • Immunosuppressive Agents / antagonists & inhibitors
  • Immunosuppressive Agents / chemistry
  • Immunosuppressive Agents / metabolism
  • Killer Cells, Natural / immunology*
  • Killer Cells, Natural / metabolism
  • Lymphocyte Activation / genetics*
  • Lymphocyte Activation / immunology
  • Lysine / genetics*
  • Lysine / metabolism
  • Melanoma, Experimental / genetics
  • Melanoma, Experimental / metabolism
  • Membrane Glycoproteins / antagonists & inhibitors
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / genetics*
  • Membrane Glycoproteins / metabolism*
  • Membrane Glycoproteins / physiology
  • Mice
  • Molecular Sequence Data
  • Protein Binding / genetics
  • Protein Binding / immunology
  • Protein Structure, Tertiary / genetics
  • Receptors, Immunologic / antagonists & inhibitors
  • Receptors, Immunologic / chemistry
  • Receptors, Immunologic / genetics*
  • Receptors, Immunologic / metabolism*
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / metabolism
  • Signaling Lymphocytic Activation Molecule Family

Substances

  • Antigens, CD
  • Antigens, Surface
  • CD244 protein, human
  • CD48 Antigen
  • CD48 protein, human
  • Cd48 protein, mouse
  • Immunosuppressive Agents
  • Membrane Glycoproteins
  • Receptors, Immunologic
  • Recombinant Fusion Proteins
  • Signaling Lymphocytic Activation Molecule Family
  • Glutamic Acid
  • Lysine
  • Alanine