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The lipopeptide antibiotic paenibacterin binds to the bacterial outer membrane and exerts bactericidal activity

En Huang1, Ahmed E Yousef

  • 1Department of Food Science and Technology, The Ohio State University, Columbus, Ohio, USA.

Applied and Environmental Microbiology
|February 25, 2014
PubMed

Insights

Paenibacterin, a lipopeptide antimicrobial, targets bacterial membranes. It disrupts the outer membrane of Gram-negative bacteria and damages the cytoplasmic membrane of both Gram-negative and Gram-positive bacteria.

Area of Science:

  • Microbiology
  • Biochemistry
  • Pharmacology

Background:

  • Paenibacterin is a broad-spectrum lipopeptide antimicrobial produced by Paenibacillus thiaminolyticus OSY-SE.
  • It features a cyclic 13-residue peptide linked to a C15 fatty acyl chain.

Purpose of the Study:

  • To investigate the mechanism of action of paenibacterin against Escherichia coli (Gram-negative) and Staphylococcus aureus (Gram-positive).

Main Methods:

  • Assessing paenibacterin's interaction with lipopolysaccharides (LPS) from E. coli.
  • Evaluating the effect of LPS on antimicrobial activity.
  • Measuring bacterial membrane potential depolarization and intracellular potassium ion leakage.

Main Results:

  • Paenibacterin exhibits strong affinity for negatively charged LPS in Gram-negative bacteria, with LPS addition neutralizing its activity against E. coli.
  • Electrostatic interaction with LPS may facilitate antibiotic uptake into Gram-negative cells.
  • Paenibacterin causes cytoplasmic membrane damage in both E. coli and S. aureus, indicated by membrane depolarization and potassium ion leakage.

Conclusions:

  • Paenibacterin's bactericidal activity stems from outer membrane disruption in Gram-negative bacteria and cytoplasmic membrane damage in both Gram-negative and Gram-positive bacteria.
  • Additional bactericidal mechanisms may also be involved.

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