Skip to main content Accessibility help

We use cookies to distinguish you from other users and to provide you with a better experience on our websites. Close this message to accept cookies or find out how to manage your cookie settings.

Close cookie message
×
  1. Home
  2. Search

Refine search

Refine search

Access:
Content type:
Publication date:
Apply   From and To filters
Subject: Show more
Journals Show more
Publishers: Show more
Societies Show more
Series: Show more
Collections: Show more

Actions for selected content:

Select all | Deselect all
  • View selected items
  • Export citations
  • Download PDF (zip)
  • Save to Kindle
  • Save to Dropbox
  • Save to Google Drive

Save Search

You can save your searches here and later view and run them again in "My saved searches".

Please provide a title, maximum of 40 characters.
Cancel
×

1 results

  • Flow Cytometry and Electron Microscopy Study of Staphylococcus aureus and Escherichia coli Treated with Mdc-Hly

  • Xuemei Lu, Xiaobao Jin, Jiayong Zhu
  • Journal:
    Microscopy and Microanalysis / Volume 21 / Issue 2 / April 2015
    Published online by Cambridge University Press:
    13 March 2015, pp. 351-357
    Print publication:
    April 2015

  • In our previous study, a novel hybrid protein combining human lysozyme (Hly) with Musca domestica cecropin (Mdc) was successfully constructed. The broad antibacterial activity against various foodborne pathogens of Mdc-hly suggests its scope as a food preservative. The aim of the present study was to investigate the antibacterial mechanism of the recombinant Mdc-hly. The damage induced by Mdc-hly on Staphylococcus aureus and Escherichia coli was investigated using flow cytometry (FC), scanning electron microscopy (SEM), and transmission electron microscopy (TEM). The results of FC showed that Mdc-hly causes bacterial membrane permeabilization. SEM and TEM studies revealed that Mdc-hly is capable of damaging both the membrane and the wall of bacteria, resulting in efflux of essential cytoplasmic contents. Both FC and EM revealed that the effects of Mdc-hly were greater than its parental peptides. Understanding the antibacterial mechanism of Mdc-hly is of a great interest in further utilization of its use in treatment of food and in clinical environments.