Characterization of a Novel Phage ΦAb1656-2 and Its Endolysin with Higher Antimicrobial Activity against Multidrug-Resistant Acinetobacter baumannii

Viruses. 2021 Sep 16;13(9):1848. doi: 10.3390/v13091848.

Abstract

Acinetobacter baumannii is a nosocomial pathogen, which is a problem worldwide due to the emergence of a difficult-to-treat multidrug-resistant A. baumannii (MDRAB). Endolysins are hydrolytic enzymes produced by a bacteriophage that can be used as a potential therapeutic agent for multidrug-resistant bacterial infection in replacing antibiotics. Here, we isolated a novel bacteriophage through prophage induction using mitomycin C from clinical A. baumannii 1656-2. Morphologically, ΦAb1656-2 was identified as a Siphoviridae family bacteriophage, which can infect MDRAB. The whole genome of ΦAb1656-2 was sequenced, and it showed that it is 50.9 kb with a G + C content of 38.6% and 68 putative open reading frames (ORFs). A novel endolysin named AbEndolysin with an N-acetylmuramidase-containing catalytic domain was identified, expressed, and purified from ΦAb1656-2. Recombinant AbEndolysin showed significant antibacterial activity against MDRAB clinical strains without any outer membrane permeabilizer. These results suggest that AbEndolysin could represent a potential antimicrobial agent for treating MDRAB clinical isolates.

Keywords: Acinetobacter baumannii; antimicrobial activity; bacteriophage; endolysin; genome sequencing.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acinetobacter Infections / microbiology
  • Acinetobacter baumannii / drug effects*
  • Acinetobacter baumannii / virology*
  • Anti-Bacterial Agents / pharmacology
  • Catalytic Domain
  • Drug Resistance, Multiple, Bacterial
  • Endopeptidases / chemistry
  • Endopeptidases / genetics
  • Endopeptidases / isolation & purification*
  • Endopeptidases / pharmacology*
  • Genome, Viral
  • Humans
  • Microbial Interactions
  • Microbial Sensitivity Tests
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / pharmacology
  • Siphoviridae / chemistry
  • Siphoviridae / genetics
  • Siphoviridae / isolation & purification*
  • Siphoviridae / physiology*
  • Viral Proteins / chemistry
  • Viral Proteins / genetics
  • Viral Proteins / isolation & purification*
  • Viral Proteins / pharmacology*
  • Whole Genome Sequencing

Substances

  • Anti-Bacterial Agents
  • Recombinant Proteins
  • Viral Proteins
  • Endopeptidases
  • endolysin, Acinetobacter baumannii phage