ArticleMicrobial biotechnology2015
Construction of a chimeric lysin Ply187N-V12C with extended lytic activity against staphylococci and streptococci.
Article in Microbial biotechnology, 2015. 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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Who cites it
28 citing papers in PubMed.
- A Rapid Molecular Detection Method for Streptococcus agalactiae Based on Bacteriophage Lysin Lysis and Real-Time PCR.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2026Article
- Effect of Domain Manipulation in the Staphylococcal Phage Endolysin, Endo88, on Lytic Efficiency and Host Range.Molecular biotechnology · 2025Article
- The Synergistic and Chimeric Mechanism of Bacteriophage Endolysins: Opportunities for Application in Biotherapeutics, Food, and Health Sectors.Probiotics and antimicrobial proteins · 2025Review
- Phage-derived proteins: Advancing food safety through biocontrol and detection of foodborne pathogens.Comprehensive reviews in food science and food safety · 2025Review
- Phage-Derived Endolysins Against Resistant Staphylococcus spp.: A Review of Features, Antibacterial Activities, and Recent Applications.Infectious diseases and therapy · 2025Review
- Identification and Characterization of a Novel Prophage Lysin againstMolecules (Basel, Switzerland) · 2024Article
- Research Progress on Strategies for Improving the Enzyme Properties of Bacteriophage Endolysins.Journal of microbiology and biotechnology · 2024Review
- Rapid Antibacterial Activity Assessment of Chimeric Lysins.International journal of molecular sciences · 2024Article
- A novel chimeric endolysin Cly2v shows potential in treating streptococci-induced bovine mastitis and systemic infections.Frontiers in microbiology · 2024Article
- Bacteriophage Endolysin: A Powerful Weapon to Control Bacterial Biofilms.The protein journal · 2023Review
- Therapeutic potential of bacteriophage endolysins for infections caused by Gram-positive bacteria.Journal of biomedical science · 2023Review
- A Highly Active Chimeric Lysin with a Calcium-Enhanced Bactericidal Activity againstAntibiotics (Basel, Switzerland) · 2021Article
- Engineered Lysins With Customized Lytic Activities Against Enterococci and Staphylococci.Frontiers in microbiology · 2020Article
- ClyJ Is a Novel Pneumococcal Chimeric Lysin with a Cysteine- and Histidine-Dependent Amidohydrolase/Peptidase Catalytic Domain.Antimicrobial agents and chemotherapy · 2019Article
- Phage Endolysins as Potential Antimicrobials against Multidrug ResistantMicroorganisms · 2019Review
- Article
- Review
- Engineering of Phage-Derived Lytic Enzymes: Improving Their Potential as Antimicrobials.Antibiotics (Basel, Switzerland) · 2018Review
- Synthetic biology of modular proteins.Bioengineered · 2017Review
- A novel chimeric lysin with robust antibacterial activity against planktonic and biofilm methicillin-resistant Staphylococcus aureus.Scientific reports · 2017Article
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Developing chimeric lysins with a wide lytic spectrum would be important for treating some infections caused by multiple pathogenic bacteria. In the present work, a novel chimeric lysin (Ply187N-V12C) was constructed by fusing the catalytic domain (Ply187N) of the bacteriophage lysin Ply187 with the cell binding domain (146-314aa, V12C) of the lysin PlyV12. The results showed that the chimeric lysin Ply187N-V12C had not only lytic activity similar to Ply187N against staphylococcal strains but also extended its lytic activity to streptococci and enterococci, such as Streptococcus dysgalactiae, Streptococcus agalactiae, Streptococcus pyogenes, Enterococcus faecium and Enterococcus faecalis, which Ply187N could not lyse. Our work demonstrated that generating novel chimeric lysins with an extended lytic spectrum was feasible through fusing a catalytic domain with a cell-binding domain from lysins with lytic spectra across multiple genera.
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