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Related Experiment Videos

Human CD4 binds immunoglobulins.

P Lenert1, D Kroon, H Spiegelberg

  • 1Department of Medicine, University of California, San Diego 92103.

Science (New York, N.Y.)
|June 29, 1990
PubMed
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T cell glycoprotein CD4 binds to immunoglobulin (Ig), a crucial interaction for HIV binding. This CD4-Ig binding is mediated by the Fab portion and localized to specific amino acids, impacting antibody-antigen complex formation.

Area of Science:

  • Immunology
  • Virology
  • Molecular Biology

Background:

  • T cell glycoprotein CD4 is known to bind to MHC class II molecules and the HIV envelope protein gp120.
  • The interaction of CD4 with other molecules is critical for immune responses and viral entry.
  • Understanding CD4's binding partners and mechanisms is essential for developing therapeutic strategies against HIV.

Purpose of the Study:

  • To investigate the binding of recombinant CD4 (rCD4) to human immunoglobulin (Ig).
  • To identify the specific regions and domains of CD4 responsible for Ig binding.
  • To explore the functional implications of CD4-Ig interaction in antibody-antigen complex formation and HIV interaction.

Main Methods:

  • Binding assays using recombinant CD4 (rCD4) and polyclonal Ig, including human myeloma proteins.

Related Experiment Videos

  • Characterization of binding dependence on Ig fragments (Fab vs. Fc) and light chain.
  • Inhibition studies using soluble rCD4, HIV gp120, and sulfated dextrans.
  • Peptide mapping using synthetic peptides to localize the Ig-binding region on CD4.

    • Main Results:

    • Recombinant CD4 (rCD4) demonstrated binding to 78% of tested human myeloma proteins and polyclonal Ig.
    • CD4-Ig binding was dependent on the Fab portion of Ig and independent of the light chain.
    • The critical region for CD4 binding to Ig was mapped to amino acids 21–38 in the first extracellular domain of CD4.
    • CD4-bound antibodies showed a 100-fold enhancement in complexing with antigen compared to antibodies alone.

    Conclusions:

    • CD4 directly binds to the Fab fragment of immunoglobulin, independent of the light chain.
    • The N-terminal region (amino acids 21–38) of CD4 is critical for this interaction.
    • CD4-Ig binding enhances antibody-antigen complex formation, potentially contributing to antibody-mediated enhancement of cellular HIV interaction.