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Related Experiment Videos

Oligodeoxynucleotides interact with recombinant CD4 at multiple sites

L Yakubov1, Z Khaled, L M Zhang

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

The Journal of Biological Chemistry
|September 5, 1993
PubMed
Summary
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Oligonucleotides modify recombinant soluble CD4 (rsCD4), revealing two binding sites with varying affinities. This finding impacts understanding of CD4 interactions and potential therapeutic strategies.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Drug Discovery

Background:

  • Recombinant soluble CD4 (rsCD4) is a key target for therapeutic interventions, particularly for HIV.
  • Understanding the binding characteristics of molecules to rsCD4 is crucial for developing effective drugs.

Purpose of the Study:

  • To investigate the specific modification of rsCD4 by alkylating oligodeoxynucleotides.
  • To identify and characterize the binding sites of oligonucleotides on rsCD4.
  • To explore potential interactions with other molecules, including therapeutic agents.

Main Methods:

  • Chemical modification of rsCD4 using 5'-alkylating oligodeoxynucleotides.
  • Saturation kinetics to determine binding site affinity.
  • Electrophoretic analysis to confirm modification and binding sites.

Related Experiment Videos

  • Competitive binding assays with non-alkylating oligonucleotides, phosphorothioate oligonucleotides, anionic dyes, and potential anti-HIV agents.

    • Main Results:

    • Specific, saturable modification of rsCD4 by alkylating oligonucleotides was observed.
    • Two binding sites on rsCD4 with apparent dissociation constants (Kd) of approximately 0.1 and 1 microM were identified.
    • Electrophoresis confirmed the presence of two distinct modified protein species.
    • Oligonucleotide binding was inhibited by excess non-alkylating and phosphorothioate oligonucleotides.
    • Interactions of rsCD4 with anionic dyes and potential anti-HIV agents were demonstrated.
    • Phosphorothioate oligonucleotides inhibited binding of rsCD4 to the L71.1.1 monoclonal antibody, which targets the CDR3-like loop.

    Conclusions:

    • Oligonucleotides bind to at least two distinct sites on the D1 domain of rsCD4.
    • These binding sites are located in remote regions, including the CDR2- and CDR3-like loops.
    • The study provides insights into the molecular interactions of CD4 and has implications for the design of oligonucleotide-based therapeutics.