The flocculating cationic polypetide from moringa oleifera seeds damages bacterial cell membranes by causing membrane fusion

Kevin Shebek, Allen B. Schantz, Ian Sines, Kathleen Lauser, Stephanie Velegol, Manish Kumar

Research output: Contribution to journalArticle

38 Scopus citations

Abstract

A cationic protein isolated from the seeds of the Moringa oleifera tree has been extensively studied for use in water treatment in developing countries and has been proposed for use in antimicrobial and therapeutic applications. However, the molecular basis for the antimicrobial action of this peptide, Moringa oleifera cationic protein (MOCP), has not been previously elucidated. We demonstrate here that a dominant mechanism of MOCP antimicrobial activity is membrane fusion. We used a combination of cryogenic electron microscopy (cryo-EM) and fluorescence assays to observe and study the kinetics of fusion of membranes in liposomes representing model microbial cells. We also conducted cryo-EM experiments on E. coli cells where MOCP was seen to fuse the inner and outer membranes. Coarse-grained molecular dynamics simulations of membrane vesicles with MOCP molecules were used to elucidate steps in peptide adsorption, stalk formation, and fusion between membranes.

Original languageEnglish (US)
Pages (from-to)4496-4502
Number of pages7
JournalLangmuir
Volume31
Issue number15
DOIs
StatePublished - Apr 21 2015

All Science Journal Classification (ASJC) codes

  • Materials Science(all)
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Spectroscopy
  • Electrochemistry

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