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Antibacterial Activity of a Novel Peptide-Modified Lysin Against Acinetobacter baumannii and Pseudomonas aeruginosa

Hang Yang1, Mengyue Wang1, Junping Yu1

  • 1Key Laboratory of Special Pathogens and Biosafety, Center for Emerging Infectious Diseases, Wuhan Institute of Virology, Chinese Academy of Sciences Wuhan, China.

Frontiers in Microbiology
|January 7, 2016
PubMed

Insights

A novel peptide-modified lysin, PlyA, shows promise against multidrug-resistant Gram-negative bacteria like Acinetobacter baumannii and Pseudomonas aeruginosa. Further optimization is needed for effectiveness in various biological environments.

Area of Science:

  • Microbiology
  • Biotechnology
  • Antimicrobial Research

Background:

  • The rise of multidrug-resistant (MDR) bacteria, including Gram-negative pathogens like Acinetobacter baumannii and Pseudomonas aeruginosa, poses a significant global health threat.
  • Natural bacteriophage lysins are effective against Gram-positive bacteria but face challenges with Gram-negative bacteria due to outer membrane barriers.
  • Antimicrobial peptides can enhance lysin activity against Gram-negative pathogens by overcoming outer membrane resistance.

Purpose of the Study:

  • To construct and evaluate a novel peptide-modified lysin (PlyA) for antibacterial activity against Gram-negative pathogens.
  • To investigate the efficacy of PlyA against Acinetobacter baumannii and Pseudomonas aeruginosa in different growth phases and conditions.
  • To assess the potential of PlyA as an alternative therapeutic agent against MDR Gram-negative infections.

Main Methods:

  • Construction of PlyA by fusing cecropin A peptide residues 1-8 with the OBPgp279 lysin.
  • Assessment of PlyA's antibacterial activity against logarithmic and stationary phase Acinetobacter baumannii and Pseudomonas aeruginosa.
  • Evaluation of PlyA's activity in the presence of outer membrane permeabilizers (EDTA, citric acid) and in various biological matrices (culture media, milk, sera).

Main Results:

  • PlyA demonstrated significant antibacterial activity against logarithmic phase Acinetobacter baumannii and Pseudomonas aeruginosa.
  • Activity of PlyA was reduced against stationary phase cells, but could be enhanced by outer membrane permeabilizers.
  • PlyA exhibited no antibacterial activity in tested biological matrices like culture media, milk, and sera.

Conclusions:

  • A novel peptide-modified lysin, PlyA, exhibits potent antibacterial activity against Gram-negative bacteria in buffer conditions.
  • Outer membrane permeabilizers can restore PlyA's efficacy against stationary phase Gram-negative bacteria.
  • Further research and optimization are required to enhance PlyA's activity and stability in diverse biological environments for therapeutic applications.
Keywords:
Acinetobacter baumanniiPseudomonas aeruginosabacteriophage lysinengineered lysinouter membrane permeabilizers (OMPs)

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