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An E. coli expression system which detoxifies the HIV protease.

B D Korant1, C J Rizzo

  • 1Central Research and Development Department, Du Pont Experimental Station, Wilmington, Delaware 19880-0328.

Biomedica Biochimica Acta
|January 1, 1991
PubMed
Summary
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Expressing HIV protease in bacteria causes cell death. Fusing HIV protease to beta-lactamase and secreting it to the periplasmic space improves solubility and activity, preventing bacterial death.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Virology

Background:

  • Bacterial expression of HIV-1 protease leads to loss of cell viability.
  • HIV-1 protease expression may cause degradation of cellular proteins in E. coli.

Purpose of the Study:

  • To develop a method to avoid bacterial cell death during HIV-1 protease expression.
  • To investigate the solubility and enzymatic activity of periplasmic HIV-1 protease.

Main Methods:

  • Engineered an expression system fusing HIV-1 protease to beta-lactamase for periplasmic secretion.
  • Assessed bacterial viability and protein degradation.
  • Measured enzymatic activity of the secreted protease.

Main Results:

Related Experiment Videos

  • Secretion of HIV-1 protease to the periplasmic space prevented bacterial loss of viability.
  • The periplasmic form of HIV-1 protease was soluble.
  • Periplasmic HIV-1 protease exhibited several-fold higher enzymatic activity compared to intracellular aggregates.

    • Conclusions:

    • Periplasmic secretion is a viable strategy to mitigate toxicity of HIV-1 protease in bacterial expression systems.
    • The strategy enhances protease solubility and enzymatic activity.
    • Discusses the potential toxicity of HIV-1 protease in infected host cells.