Diphtheria toxin-related cytokine fusion proteins: elongation factor 2 as a target for the treatment of neoplastic disease

Mol Cell Biochem. 1994 Sep;138(1-2):151-6. doi: 10.1007/BF00928457.

Abstract

We have used protein engineering and recombinant DNA methodologies in order to construct a fusion protein in which human interleukin-2 (IL-2) is genetically linked to the catalytic and transmembrane domains of diphtheria toxin. The fusion toxin, DAB486IL-2, is highly cytotoxic for only those cells which display the high affinity interleukin-2 receptor (IL-2R) on their surface. In phase I/II clinical studies the intravenous administration of DAB486IL-2 has been found to be safe, well tolerated and may lead to the induction of durable remissions in patients presenting with a variety of IL-2R positive lymphomas.

Publication types

  • Clinical Trial
  • Clinical Trial, Phase I
  • Clinical Trial, Phase II
  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Antineoplastic Agents / pharmacology*
  • Catalysis
  • Diphtheria Toxin / chemistry*
  • Humans
  • Models, Molecular
  • Peptide Elongation Factor 2
  • Peptide Elongation Factors / drug effects*
  • Protein Engineering*
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins / pharmacology*

Substances

  • Antineoplastic Agents
  • Diphtheria Toxin
  • Peptide Elongation Factor 2
  • Peptide Elongation Factors
  • Recombinant Fusion Proteins