Antibacterial properties of Acinetobacter baumannii phage Abp1 endolysin (PlyAB1)

BMC Infect Dis. 2014 Dec 12:14:681. doi: 10.1186/s12879-014-0681-2.

Abstract

Background: Acinetobacter baumannii has emerged as one of the most important hospital-acquired pathogens in the world, because of its resistance to almost all available antibiotic drugs. Endolysins from phages are attracting increasing interest as potential antimicrobial agents, especially for drug-resistant bacteria. We previously isolated and characterized Abp1, a virulent phage targeting the multidrug-resistant A. baumannii strain, AB1.

Methods: To evaluate the antimicrobial potential of endolysin from the Abp1 phage, the endolysin gene plyAB1 was cloned and over-expressed in Escherichia coli, and the lytic activity of the recombinant protein (PlyAB1) was tested by turbidity assessment and bacteria counting assays.

Results: PlyAB1 exhibits a marked lytic activity against A. baumannii AB1, as shown by a decrease in the number of live bacteria following treatment with the enzyme. Moreover, PlyAB1 displayed a highly specific lytic effect against all of the 48 hospital-derived pandrug-resistant A. baumannii isolates that were tested. These isolates were shown to belong to different ST clones by multilocus sequence typing.

Conclusions: The results presented here show that PlyAB1 has potential as an antibiotic against drug-resistant A. baumannii.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acinetobacter baumannii / drug effects*
  • Acinetobacter baumannii / virology
  • Anti-Bacterial Agents / pharmacology*
  • Bacteriophages / enzymology*
  • Drug Resistance, Bacterial
  • Endopeptidases / pharmacology*
  • Recombinant Proteins / pharmacology
  • Viral Proteins / pharmacology*

Substances

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