ArticlePLoS pathogens2020
Structural and functional insights into a novel two-component endolysin encoded by a single gene in Enterococcus faecalis phage.
Article in PLoS pathogens, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Data mining reveals the diversity of prophage endolysins targeting pathogenic enterococci.The Journal of general virology · 2026Article
- First experimentally characterised Proteus phage endolysins have distinct metal cofactor dependencies.Applied microbiology and biotechnology · 2026Article
- Structural and functional analysis reveals the catalytic mechanism and substrate binding mode of the broad-spectrum endolysin Ply2741.Virulence · 2025Article
- Comparative antibacterial activity of N-terminal and C-terminal domains of a recombinant endolysin againstApplied and environmental microbiology · 2025Article
- Enzymatic property and stabilization mechanism of LysBT1, a novel polyextremotolerant endolysin with a C-terminal S-layer homology domain.Applied and environmental microbiology · 2025Article
- The Unique Capability of Endolysin to Tackle Antibiotic Resistance: Cracking the Barrier.Journal of xenobiotics · 2025Review
- Heterodimerization of staphylococcal phage φ2638A endolysin isoforms and their functional role in bacterial lysis.microLife · 2025Article
- Identification of cell wall binding domains and repeats inBiochemistry and biophysics reports · 2024Article
- Mechanistic basis for the allosteric activation of NADase activity in the Sir2-HerA antiphage defense system.Nature communications · 2024Article
- Characteristics of the Enterococcus Phage vB_EfS_SE, and the Properties of Its Chimeric Endolysins Harboring a PlySE-Carbohydrate-Binding Domain and a Synthetic Enzymatic Domain.Pharmaceutics · 2024Article
- Characterization of Two Novel Endolysins from Bacteriophage PEF1 and Evaluation of Their Combined Effects on the Control ofAntibiotics (Basel, Switzerland) · 2024Article
- Agents Targeting the Bacterial Cell Wall as Tools to Combat Gram-Positive Pathogens.Molecules (Basel, Switzerland) · 2024Review
- Engineering strategies and challenges of endolysin as an antibacterial agent against Gram-negative bacteria.Microbial biotechnology · 2024Review
- Fermentation Practices Select for Thermostable Endolysins in Phages.Molecular biology and evolution · 2024Article
- Structural basis of antiphage immunity generated by a prokaryotic Argonaute-associated SPARSA system.Nature communications · 2024Article
- A novel chimeric endolysin Cly2v shows potential in treating streptococci-induced bovine mastitis and systemic infections.Frontiers in microbiology · 2024Article
- Identification and classification of papain-like cysteine proteinases.The Journal of biological chemistry · 2023Article
- Understanding the Molecular Basis for Homodimer Formation of the Pneumococcal Endolysin Cpl-1.ACS infectious diseases · 2023Article
- On the Occurrence and Multimerization of Two-Polypeptide Phage Endolysins Encoded in Single Genes.Microbiology spectrum · 2022Article
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9 authors.
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Abstract
Using bacteriophage-derived endolysins as an alternative strategy for fighting drug-resistant bacteria has recently been garnering renewed interest. However, their application is still hindered by their narrow spectra of activity. In our previous work, we demonstrated that the endolysin LysIME-EF1 possesses efficient bactericidal activity against multiple strains of Enterococcus faecalis (E. faecalis). Herein, we observed an 8 kDa fragment and hypothesized that it contributes to LysIME-EF1 lytic activity. To examine our hypothesis, we determined the structure of LysIME-EF1 at 1.75 Å resolution. LysIME-EF1 exhibits a unique architecture in which one full-length LysIME-EF1 forms a tetramer with three additional C-terminal cell-wall binding domains (CBDs) that correspond to the abovementioned 8 kDa fragment. Furthermore, we identified an internal ribosomal binding site (RBS) and alternative start codon within LysIME-EF1 gene, which are demonstrated to be responsible for the translation of the truncated CBD. To elucidate the molecular mechanism for the lytic activity of LysIME-EF1, we combined mutagenesis, lytic activity assays and in vivo animal infection experiments. The results confirmed that the additional LysIME-EF1 CBDs are important for LysIME-EF1 architecture and its lytic activity. To our knowledge, this is the first determined structure of multimeric endolysin encoded by a single gene in E. faecalis phages. As such, it may provide valuable insights into designing potent endolysins against the opportunistic pathogen E. faecalis.
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