Antimicrobial nodule-specific cysteine-rich peptides disturb the integrity of bacterial outer and inner membranes and cause loss of membrane potential

Ann Clin Microbiol Antimicrob. 2016 Jul 28;15(1):43. doi: 10.1186/s12941-016-0159-8.

Abstract

Background: Certain legume plants produce a plethora of AMP-like peptides in their symbiotic cells. The cationic subgroup of the nodule-specific cysteine-rich (NCR) peptides has potent antimicrobial activity against gram-negative and gram-positive bacteria as well as unicellular and filamentous fungi.

Findings: It was shown by scanning and atomic force microscopies that the cationic peptides NCR335, NCR247 and Polymyxin B (PMB) affect differentially on the surfaces of Sinorhizobium meliloti bacteria. Similarly to PMB, both NCR peptides caused damages of the outer and inner membranes but at different extent and resulted in the loss of membrane potential that could be the primary reason of their antimicrobial activity.

Conclusions: The primary reason for bacterial cell death upon treatment with cationic NCR peptides is the loss of membrane potential.

Keywords: Antimicrobial activity; Atomic force and scanning electron microscopy; Membrane disruption.

MeSH terms

  • Antimicrobial Cationic Peptides / metabolism
  • Antimicrobial Cationic Peptides / pharmacology*
  • Cell Membrane / drug effects*
  • Cell Membrane / ultrastructure
  • Medicago truncatula / physiology
  • Membrane Potentials / drug effects*
  • Microscopy, Atomic Force
  • Microscopy, Electron, Scanning
  • Plant Proteins / metabolism
  • Plant Proteins / pharmacology*
  • Polymyxin B / pharmacology
  • Root Nodules, Plant / physiology
  • Sinorhizobium meliloti / drug effects*
  • Sinorhizobium meliloti / growth & development
  • Sinorhizobium meliloti / ultrastructure

Substances

  • Antimicrobial Cationic Peptides
  • Plant Proteins
  • Polymyxin B