Antibacterial activity and modes of action of phosvitin-derived peptide Pt5e against clinical multi-drug resistance bacteria

Fish Shellfish Immunol. 2016 Nov:58:370-379. doi: 10.1016/j.fsi.2016.09.044. Epub 2016 Sep 22.

Abstract

Pt5e, a mutant peptide derived from the C-terminal 55 residues of zebrafish phosvitin, has been suggested to be a novel antibacterial peptide. However, if it is applicable to clinical MDR bacteria remains to be tested. In this study, high-purity Pt5e was first expressed and purified by fusion with cationic elastin-like polypeptide. Pt5e was then shown to be capable of effectively killing all the five clinical MDR bacteria tested. Pt5e kill the MDR bacteria at several levels, including inserting into the bacterial membranes, causing the membrane depolarization and permeabilization, and inducing the intracellular apoptosis/necrosis. All these data suggest that Pt5e is a promising therapeutic potential as an antibiotics against clinical MDR bacteria.

Keywords: Antibiotics; Antimicrobial peptide; Multi-drug resistance bacteria; Phosvitin; Zebrafish.

MeSH terms

  • Acinetobacter baumannii / drug effects
  • Animals
  • Anti-Bacterial Agents / pharmacology*
  • Antimicrobial Cationic Peptides / pharmacology
  • Bacteria / drug effects*
  • Drug Resistance, Multiple / drug effects*
  • Escherichia coli / drug effects
  • Klebsiella pneumoniae / drug effects
  • Phosvitin / pharmacology*
  • Recombinant Proteins / pharmacology
  • Zebrafish / metabolism*
  • Zebrafish Proteins / pharmacology*

Substances

  • Anti-Bacterial Agents
  • Antimicrobial Cationic Peptides
  • Recombinant Proteins
  • Zebrafish Proteins
  • Phosvitin