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Receptor-based antidote for diphtheria.

Jeong-Heon Cha1, Joanna S Brooke, Mee Young Chang

  • 1Department of Microbiology, The University of Texas Southwestern Medical Center, Dallas, Texas 75390-9048, USA.

Infection and Immunity
|April 16, 2002
PubMed
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Researchers developed a novel diphtheria toxin (DT) antidote using a modified human heparin-binding growth factor (HB-EGF) precursor. This engineered protein effectively neutralizes DT without causing serum sickness or tumor growth, offering a safer treatment for diphtheria.

Area of Science:

  • Biochemistry
  • Toxicology
  • Molecular Biology

Background:

  • Equine diphtheria antitoxin, a common treatment for human diphtheria, can cause adverse serum sickness reactions.
  • The diphtheria toxin (DT) receptor, also known as the heparin-binding epidermal growth factor-like growth factor (HB-EGF) precursor, is crucial for DT binding to cells.

Purpose of the Study:

  • To develop a safer and more effective alternative to equine antitoxin for treating human diphtheria.
  • To engineer a soluble receptor analog of the DT receptor/HB-EGF precursor that can neutralize DT without adverse effects.

Main Methods:

  • Recombinant mature human HB-EGF was used as a soluble receptor analog to bind radioiodinated DT.
  • A truncated HB-EGF mutant (residues 106-149) lacking the heparin-binding domain was engineered to prevent cell association.

Related Experiment Videos

  • Further modifications were made to the EGF-like domain (I117A/L148A) to reduce mitogenic potential.
  • Surface plasmon resonance was used to confirm binding affinity.

    • Main Results:

    • Recombinant mature HB-EGF successfully bound radioiodinated DT, inhibiting its cellular binding.
    • The truncated HB-EGF (106-149) demonstrated heparin-independent DT binding and was a more effective inhibitor than mature HB-EGF.
    • The modified truncated HB-EGF (I117A/L148A) exhibited significantly reduced mitogenic activity while retaining high DT binding affinity.

    Conclusions:

    • The truncated (I117A/L148A) HB-EGF protein acts as a potent DT-neutralizing agent.
    • This engineered protein shows potential as a safe and effective antidote for human diphtheria, avoiding the risks associated with equine antitoxin.