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Clostridium perfringens Virulent Bacteriophage CPS2 and Its Thermostable Endolysin LysCPS2

Eunsu Ha1,2, Bokyung Son3,4, Sangryeol Ryu5,6

  • 1Department of Food and Animal Biotechnology, Seoul National University, Seoul 08826, Korea. esha0521@gmail.com.

Viruses
|May 13, 2018
PubMed

Insights

A novel bacteriophage, CPS2, was isolated from chicken feces to combat multidrug-resistant Clostridium perfringens. Its endolysin, LysCPS2, exhibits potent, thermostable lytic activity against C. perfringens, offering a promising biocontrol alternative.

Area of Science:

  • Microbiology
  • Bacteriophage Therapy
  • Enzymology

Background:

  • Clostridium perfringens is a major cause of foodborne illness.
  • Multidrug-resistant bacteria necessitate alternative antimicrobial strategies.
  • Bacteriophages offer a potential solution for combating bacterial infections.

Purpose of the Study:

  • To isolate and characterize a bacteriophage specific to C. perfringens.
  • To investigate the lytic activity and properties of its endolysin.
  • To evaluate the potential of the endolysin as a biocontrol agent.

Main Methods:

  • Isolation and characterization of bacteriophage CPS2 from chicken feces.
  • Genomic analysis of the CPS2 bacteriophage.
  • Purification and biochemical characterization of the putative endolysin LysCPS2.
  • Assay of lytic activity against C. perfringens under various conditions.

Main Results:

  • A virulent C. perfringens-specific bacteriophage, CPS2, was identified.
  • The endolysin LysCPS2 demonstrated strong lytic activity against C. perfringens.
  • LysCPS2 showed high thermostability and broad NaCl tolerance.
  • The enzyme's cell wall binding domain exhibited specificity for C. perfringens.

Conclusions:

  • LysCPS2 is a highly thermostable endolysin with specific activity against C. perfringens.
  • This endolysin represents a novel biocontrol agent for C. perfringens.
  • The findings support the development of phage-derived enzymes as alternatives to antibiotics.
Keywords:
Clostridium perfringensbacteriophageendolysin

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