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LysPBC2, a Novel Endolysin Harboring a Bacillus cereus Spore Binding Domain
Minsuk Kong1,2,3,4, Hongjun Na1,2,3,4, Nam-Chul Ha1,2,3,4
1Department of Food and Animal Biotechnology, Seoul National University, Seoul, South Korea.
Applied and Environmental Microbiology
|December 16, 2018
Summary
A novel endolysin, LysPBC2, shows broad lytic activity against Bacillus, Listeria, and Clostridium species. Mutations enhancing its lytic activity against Bacillus cereus also reduced its thermal stability, offering insights for antimicrobial development.
Area of Science:
- Microbiology
- Biochemistry
- Molecular Biology
Background:
- Bacteriophage-derived endolysins are potent lytic enzymes with potential as antibiotic alternatives.
- Understanding endolysin domain function is crucial for developing effective therapeutics against Gram-positive bacteria.
- Bacillus cereus is a spore-forming pathogen requiring novel control strategies.
Purpose of the Study:
- To isolate and characterize a novel endolysin, LysPBC2, from a Bacillus cereus phage.
- To investigate the lytic activity, host range, and domain functions of LysPBC2.
- To explore the potential of LysPBC2 and its derivatives as antimicrobials against Bacillus cereus.
Main Methods:
- Isolation and characterization of Bacillus cereus phage PBC2 and its endolysin LysPBC2.
- Determination of LysPBC2's lytic activity spectrum against various bacterial species.
- Site-directed mutagenesis to identify key residues for catalytic and spore-binding activities.
- Immunogold electron microscopy and binding assays to localize the spore binding domain (SBD).
Main Results:
- LysPBC2 exhibits broad lytic activity against Bacillus, Listeria, and Clostridium species, exceeding the phage's host range.
- The SBD of LysPBC2 specifically binds to Bacillus cereus spores, localizing to the spore cortex layer.
- Mutagenesis studies revealed essential residues for catalytic and SBD functions.
- Derivatives with impaired SBD showed enhanced lytic activity against vegetative Bacillus cereus cells but reduced thermal stability.
Conclusions:
- LysPBC2 is a potent endolysin with broad-spectrum activity and a unique SBD.
- The SBD plays a role in LysPBC2 structure stabilization and influences lytic activity.
- Understanding LysPBC2's domain functions provides a basis for designing targeted antimicrobials and diagnostic tools for Bacillus cereus control.
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