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Related Experiment Videos

Recombinant, truncated CD4 molecule (rT4) binds IgG.

S Lederman1, M J Yellin, A M Cleary

  • 1Department of Medicine, Columbia University, College of Physicians and Surgeons, New York, NY 10032.

Journal of Immunology (Baltimore, Md. : 1950)
|January 1, 1990
PubMed
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The CD4 molecule, specifically its truncated form (rT4), directly interacts with Immunoglobulin G (IgG) via its Fc region. This binding is specific and not inhibited by anti-CD4 antibodies, suggesting a novel interaction pathway.

Area of Science:

  • Immunology
  • Molecular Biology

Background:

  • CD4 is a T lymphocyte surface glycoprotein crucial for B cell activation.
  • A truncated form of CD4 (rT4) unexpectedly bound to antibodies.

Purpose of the Study:

  • To investigate the interaction between rT4 and Immunoglobulin (Ig) molecules.
  • To determine if CD4 (rT4) specifically binds to IgG.

Main Methods:

  • Enzyme-linked immunosorbent assay (ELISA) to detect binding.
  • Using purified human IgG, myeloma proteins, and different Ig isotypes.
  • Testing binding with aggregated IgG and IgG fragments (Fc and F(ab)2).

Main Results:

  • rT4 demonstrated dose-dependent binding to purified human IgG.

Related Experiment Videos

  • Binding specificity was confirmed for IgG, excluding IgM, IgA, IgD, and beta 2-microglobulin.
  • rT4 bound IgG Fc fragments but not F(ab)2 fragments, and showed increased avidity for aggregated IgG.

    • Conclusions:

    • The CD4 molecule (rT4) specifically interacts with a conserved structure on the IgG Fc region.
    • This interaction is independent of anti-CD4 antibodies and suggests a novel binding mechanism.