Next Article in Journal
Genome Sequences of Akhmeta Virus, an Early Divergent Old World Orthopoxvirus
Next Article in Special Issue
Nanomedicine and Phage Capsids
Previous Article in Journal
Single Viruses on the Fluorescence Microscope: Imaging Molecular Mobility, Interactions and Structure Sheds New Light on Viral Replication
Previous Article in Special Issue
Exploiting a Phage-Bacterium Interaction System as a Molecular Switch to Decipher Macromolecular Interactions in the Living Cell
Article Menu
Issue 5 (May) cover image

Export Article

Open AccessArticle

Clostridium perfringens Virulent Bacteriophage CPS2 and Its Thermostable Endolysin LysCPS2

1,2,†, 1,2,† and 1,2,*
Department of Food and Animal Biotechnology, Seoul National University, Seoul 08826, Korea
Department of Agricultural Biotechnology, and Research Institute of Agriculture and Life Sciences, Seoul National University, Seoul 08826, Korea
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Viruses 2018, 10(5), 251;
Received: 4 April 2018 / Revised: 10 May 2018 / Accepted: 11 May 2018 / Published: 11 May 2018
(This article belongs to the Special Issue Biotechnological Applications of Phage and Phage-Derived Proteins)
PDF [1945 KB, uploaded 11 May 2018]


Clostridium perfringens is one of the most common causes of food-borne illness. The increasing prevalence of multidrug-resistant bacteria requires the development of alternatives to typical antimicrobial treatments. Here, we isolated and characterized a C. perfringens-specific virulent bacteriophage CPS2 from chicken feces. The CPS2 phage contains a 17,961 bp double-stranded DNA genome with 25 putative ORFs, and belongs to the Picovirinae, subfamily of Podoviridae. Bioinformatic analysis of the CPS2 genome revealed a putative endolysin, LysCPS2, which is homologous to the endolysin of Clostridium phage phiZP2 and phiCP7R. The enzyme showed strong lytic activity against C. perfringens with optimum conditions at pH 7.5–10, 25–65 °C, and over a broad range of NaCl concentrations. Interestingly, LysCPS2 was found to be highly thermostable, with up to 30% of its lytic activity remaining after 10 min of incubation at 95 °C. The cell wall binding domain in the C-terminal region of LysCPS2 showed a binding spectrum specific to C. perfringens strains. This is the first report to characterize highly thermostable endolysin isolated from virulent C. perfringens bacteriophage. The enzyme can be used as an alternative biocontrol and detection agent against C. perfringens. View Full-Text
Keywords: bacteriophage; endolysin; Clostridium perfringens bacteriophage; endolysin; Clostridium perfringens

Graphical abstract

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Share & Cite This Article

MDPI and ACS Style

Ha, E.; Son, B.; Ryu, S. Clostridium perfringens Virulent Bacteriophage CPS2 and Its Thermostable Endolysin LysCPS2. Viruses 2018, 10, 251.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Viruses EISSN 1999-4915 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top