LysSAP26, a New Recombinant Phage Endolysin with a Broad Spectrum Antibacterial Activity

Viruses. 2020 Nov 23;12(11):1340. doi: 10.3390/v12111340.

Abstract

Multidrug-resistant (MDR) bacteria are a major threat to public health. Bacteriophage endolysins (lysins) are a promising alternative treatment to traditional antibiotics. However, the lysins currently under development are still underestimated. Herein, we cloned the lysin from the SAP-26 bacteriophage genome. The recombinant LysSAP26 protein inhibited the growth of carbapenem-resistant Acinetobacter baumannii, Escherichia coli, Klebsiella pneumoniae, and Pseudomonas aeruginosa, oxacillin-resistant Staphylococcus aureus, and vancomycin-resistant Enterococcus faecium with minimum inhibitory concentrations of 5~80 µg/mL. In animal experiments, mice infected with A. baumannii were protected by LysSAP26, with a 40% survival rate. Transmission electron microscopy analysis confirmed that LysSAP26 treatment resulted in the destruction of bacterial cell walls. LysSAP26 is a new endolysin that can be applied to treat MDR A. baumannii, E. faecium, S. aureus, K. pneumoniae, P. aeruginosa, and E. coli infections, targeting both Gram-positive and Gram-negative bacteria.

Keywords: antimicrobial activity; endolysin; multidrug-resistant bacteria.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Anti-Bacterial Agents / pharmacology*
  • Bacteriophages / enzymology*
  • Drug Resistance, Multiple, Bacterial
  • Endopeptidases / genetics*
  • Endopeptidases / pharmacology*
  • Female
  • Gram-Negative Bacteria / drug effects*
  • Gram-Positive Bacteria / drug effects*
  • Mice
  • Mice, Inbred BALB C
  • Microbial Sensitivity Tests
  • Neutropenia
  • Recombinant Proteins / pharmacology
  • Viral Proteins / genetics
  • Viral Proteins / pharmacology

Substances

  • Anti-Bacterial Agents
  • Recombinant Proteins
  • Viral Proteins
  • Endopeptidases
  • endolysin