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Updated: Aug 5, 2026
09:44
Characterization of a Pathogenic Escherichia coli Strain Derived from Oreochromis spp. Farms Using Whole-Genome Sequencing
Published on: December 23, 2022
Data mining reveals the diversity of prophage endolysins targeting pathogenic enterococci
Finn O'Dea1,2, Andrew Kinsella3, Brooks J Rady1,2
1Molecular Microbiology, School of Biosciences, University of Sheffield, Sheffield, UK.
The Journal of General Virology
|July 17, 2026
Summary
Antimicrobial resistance is a global threat. Researchers analyzed over 48,000 enterococcal prophage endolysins, discovering 33 unique domain architectures to aid in developing new enzybiotics against resistant bacteria.
Area of Science:
- Microbiology
- Genomics
- Biotechnology
Background:
- Antimicrobial resistance (AMR) is a major global health concern, with enterococci being significant contributors due to their antibiotic resistance.
- Alternative therapeutics are crucial for treating multidrug-resistant enterococcal infections in both human and agricultural settings.
- Bacteriophage-derived endolysins show promise as antibacterial agents, but limited diversity and phage resistance are application challenges.
Purpose of the Study:
- To conduct a large-scale analysis of prophage-encoded endolysins in key enterococcal species.
- To characterize the diversity of catalytic and cell wall-binding domains (CBDs) within these endolysins.
- To identify novel endolysin structures for the development of next-generation enzybiotics.
Main Methods:
- Bioinformatic analysis of over 48,000 prophage sequences from *Enterococcus faecalis*, *Enterococcus faecium*, and *Enterococcus cecorum*.
- Identification and classification of distinct endolysin domain architectures.
- Characterization of catalytic and cell wall-binding domains (CBDs), including novel putative domains.
Main Results:
- Identification of 33 distinct endolysin domain architectures across the studied enterococcal pathogens.
- Discovery of diverse combinations of catalytic and cell wall-binding domains (CBDs).
- Characterization of novel putative CBDs, expanding the known repertoire of enterococcal lysins.
Conclusions:
- The study significantly expands the known diversity of enterococcal prophage-encoded endolysins.
- Findings provide a comprehensive resource for the rational design of recombinant enzybiotics.
- This research facilitates the development of novel therapeutics to combat multidrug-resistant enterococcal infections.
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