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Antimicrobial activity and synergistic effect of phage-encoded antimicrobial peptides with colistin and outer

Punnaphat Rothong1, Udomluk Leungtongkam1, Supat Khongfak2

  • 1Department of Microbiology and Parasitology, Faculty of Medical Science, Naresuan University, Muang, Phitsanulok, Thailand.

Peerj
|December 30, 2024
PubMed
Abstract

Insights

Phage-encoded antimicrobial peptides show potent activity against multidrug-resistant Acinetobacter baumannii. These peptides are safe for therapeutic use and effectively combat biofilms and infections.

Area of Science:

  • Microbiology
  • Biotechnology
  • Drug Discovery

Background:

  • Acinetobacter baumannii is a major public health concern due to its increasing antibiotic resistance.
  • Phage-encoded antimicrobial peptides (AMPs) offer a promising alternative to traditional antibiotics against resistant bacteria.

Purpose of the Study:

  • To design and evaluate antimicrobial peptides derived from Acinetobacter baumannii bacteriophage endolysins.
  • To assess the efficacy, synergy, biofilm inhibition, and safety of these novel peptides.

Main Methods:

  • Peptides were designed from bacteriophage endolysins.
  • Minimum inhibitory concentration (MIC), synergistic effects with colistin and citric acid, cytotoxicity, biofilm inhibition, and Galleria mellonella infection models were evaluated.

Main Results:

  • Three peptides (PE04-1, PE04-1(NH2), PE04-2) showed significant antimicrobial activity against multidrug-resistant (MDR) and extensively drug-resistant (XDR) bacteria.
  • Peptides demonstrated strong synergistic effects with colistin and citric acid, potent biofilm inhibition, and improved survival rates in G. mellonella models with no observed cytotoxicity.

Conclusions:

  • Phage-derived peptides are effective against MDR/XDR Acinetobacter baumannii and other pathogens.
  • These peptides represent a safe and innovative therapeutic strategy for combating antibiotic-resistant infections.
Keywords:
Acinetobacter baumanniiAntimicrobial activityBacteriophageBiofilmColistinEndolysinG. mellonella assayOuter membrane permeabilizing agentsPhage-encoded peptide

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