Interleukin 2-Bax: A novel prototype of human chimeric proteins for targeted therapy

Rami Aqeilan, Shai Yarkoni, Haya Lorberboum-Galski*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

36 Scopus citations

Abstract

During the past few years many chimeric proteins have been developed to target and kill cells expressing specific surface molecules. Generally, these molecules carry a bacterial or plant toxin that destroys the unwanted cells. The major obstacle in the clinical application of such chimeras is their immunogenicity and non-specific toxicity. We have developed a new generation of chimeric proteins, taking advantage of apoptosis-inducing proteins, such as the human Bax protein, as novel killing components. The first prototype chimeric protein, IL2-Bax, directed toward IL2R-expressing cells, was constructed, expressed in Escherichia coli and partially purified. IL2-Bax increased the population of apoptotic cells in a variety of target T cell lines, as well as in human fresh PHA-activated lymphocytes, in a dose-dependent manner and had no effect on cells lacking IL2R expression. The IL2-Bax chimera represents an innovative approach for constructing chimeric proteins comprising a molecule that binds a specific cell type and an apoptosis-inducing protein. Such new chimeric proteins could be used for targeted treatment of human diseases. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageAmerican English
Pages (from-to)271-276
Number of pages6
JournalFEBS Letters
Volume457
Issue number2
DOIs
StatePublished - 27 Aug 1999

Bibliographical note

Funding Information:
We thank Y. Azar for assistance with cell cultures. This work was supported by MTR Technologies Inc.

Keywords

  • Apoptosis
  • Bax
  • Chimeric protein
  • Interleukin 2
  • Targeted therapy

Fingerprint

Dive into the research topics of 'Interleukin 2-Bax: A novel prototype of human chimeric proteins for targeted therapy'. Together they form a unique fingerprint.

Cite this