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A Fluorescence-Based Assay of Membrane Potential for High-Throughput Functional Study of Two Endogenous Ion Channels in Two Epithelial Cell Lines
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Membrane Potential Is Required for MurJ Function.

Frederick A Rubino1, Sujeet Kumar2, Natividad Ruiz2

  • 1Department of Chemistry and Chemical Biology , Harvard University , Cambridge , Massachusetts 02138 , United States.

Journal of the American Chemical Society
|March 21, 2018
PubMed
Summary
This summary is machine-generated.

New antibiotics targeting MurJ (a flippase) are crucial for Gram-negative infections. Researchers developed a novel assay to quantify MurJ inhibition by measuring Lipid II accumulation, aiding antibiotic development.

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Area of Science:

  • Microbiology
  • Biochemistry
  • Drug Discovery

Background:

  • MurJ is a bacterial flippase essential for exporting Lipid II, a key component of the cell wall.
  • Developing new antibiotics against Gram-negative bacteria is a critical unmet medical need.
  • Existing methods to quantify MurJ activity are limited due to the lack of substrate chemical alteration during transport.

Purpose of the Study:

  • To develop a quantitative assay for monitoring MurJ flippase activity.
  • To identify conditions and compounds that inhibit MurJ function.
  • To understand the conformational changes of MurJ in response to inhibition.

Main Methods:

  • A biotin-tagging strategy was employed to quantify intracellular accumulation of Lipid II as a measure of MurJ inhibition.
  • The assay was used to test the effect of membrane potential on MurJ activity.
  • Cysteine accessibility probing was performed to analyze MurJ conformation.

Main Results:

  • A novel assay successfully quantified MurJ inhibition by measuring intracellular Lipid II accumulation.
  • MurJ activity was inhibited by compounds that dissipate the membrane potential.
  • Inhibition under membrane potential dissipation led to MurJ adopting an inactive, outward-facing conformation.

Conclusions:

  • Membrane potential is essential for MurJ function in *E. coli*.
  • The developed assay allows for the quantification of MurJ inhibitors.
  • The inactive, outward-facing conformation of MurJ provides a structural target for novel antibiotic design.