ArticleJournal of microbiology (Seoul, Korea)2017
The antibacterial activity of E. coli bacteriophage lysin lysep3 is enhanced by fusing the Bacillus amyloliquefaciens bacteriophage endolysin binding domain D8 to the C-terminal region.
Article in Journal of microbiology (Seoul, Korea), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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28 citing papers in PubMed, 45 citations in OpenAlex.
- Isolation and identification of Salmonella pullorum bacteriophage YSP2 and its use as a therapy for chicken diarrhea.Virus genes · 2018Trial
- Evaluation of the Therapeutic Effect of a Bovine-DerivedMicroorganisms · 2026Article
- Perspective Approaches to "Trojan Horse" Strategy Development for Combating Bacterial Pathogens.Pharmaceuticals (Basel, Switzerland) · 2026Review
- Review
- Characterization of LysBM1, a novel high-penetrating phage lysin targeting enterohemorrhagicFrontiers in veterinary science · 2025Article
- Endolysins and membrane-active peptides: innovative engineering strategies against gram-negative bacteria.Frontiers in microbiology · 2025Review
- New-Generation Antibacterial Agent-Cellulose-Binding Thermostable TP84_Endolysin.International journal of molecular sciences · 2024Article
- Biological and genomic characterization of a polyvalent phage PSH-1 against multidrug-resistant Salmonella Enteritidis.BMC microbiology · 2024Article
- Engineering strategies and challenges of endolysin as an antibacterial agent against Gram-negative bacteria.Microbial biotechnology · 2024Review
- Role of hypothetical protein PA1-LRP in antibacterial activity of endolysin from a newFrontiers in microbiology · 2024Article
- Characterization ofFrontiers in microbiology · 2024Article
- Development of a Magnetic Bead-Based Method for Specific Detection ofJournal of microbiology and biotechnology · 2023Article
- Article
- Beyond antibiotics: phage-encoded lysins against Gram-negative pathogens.Frontiers in microbiology · 2023Review
- Characterization of Salmonella endolysin XFII produced by recombinant Escherichia coli and its application combined with chitosan in lysing Gram-negative bacteria.Microbial cell factories · 2022Article
- Complete genome sequencing of aFrontiers in microbiology · 2022Article
- How Good are Bacteriophages as an Alternative Therapy to Mitigate Biofilms of Nosocomial Infections.Infection and drug resistance · 2022Review
- Isolation ofFrontiers in microbiology · 2022Article
- Review
- The endolysin of the Acinetobacter baumannii phage vB_AbaP_D2 shows broad antibacterial activity.Microbial biotechnology · 2021Article
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteriophage endolysin is one of the most promising antibiotic substitutes, but in Gram-negative bacteria, the outer membrane prevents the lysin from hydrolyzing peptidoglycans and blocks the development of lysin applications. The prime strategy for new antibiotic substitutes is allowing lysin to access the peptidoglycan from outside of the bacteria by reformation of the lysin. In this study, the novel Escherichia coli (E. coli) phage lyase lysep3, which lacks outside-in catalytic ability, was fused with the N-terminal region of the Bacillus amyloliquefaciens lysin including its cell wall binding domain D8 through the best manner of protein fusion based on the predicted tertiary structure of lysep3-D8 to obtain an engineered lysin that can lyse bacteria from the outside. Our results showed that lysep3-D8 could lyse both Gramnegative and Gram-positive bacteria, whereas lysep3 and D8 have no impact on bacterial growth. The MIC of lysep3-D8 on E. coli CVCC1418 is 60 μg/ml; lysep3-D8 can inhibit the growth of bacteria up to 12 h at this concentration. The bactericidal spectrum of lysep3-D8 is broad, as it can lyse of all of 14 E. coli strains, 3 P. aeruginosa strains, 1 Acinetobacter baumannii strain, and 1 Streptococcus strain. Lysep3-D8 has sufficient bactericidal effects on the 14 E. coli strains tested at the concentration of 100 μg/ml. The cell wall binding domain of the engineered lysin can destroy the integrity of the outer membrane of bacteria, thus allowing the catalytic domain to reach its target, peptidoglycan, to lyse the bacteria. Lysep3-D8 can be used as a preservative in fodder to benefit the health of animals. The method we used here proved to be a successful exploration of the reformation of phage lysin.
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