ArticleScientific reports2017
Deciphering how Cpl-7 cell wall-binding repeats recognize the bacterial peptidoglycan.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 31 citations in OpenAlex.
- Data mining reveals the diversity of prophage endolysins targeting pathogenic enterococci.The Journal of general virology · 2026Article
- Integrated computational and experimental benchmarking of Bacillus phage endolysins reveals the relationship between peptidoglycan-fragment recognition descriptors and antibacterial performance.Scientific reports · 2026Article
- Novel endolysin fromJournal of microbiology and biotechnology · 2025Article
- Bacteriophage-derived endolysins as innovative antimicrobials against bovine mastitis-causing streptococci and staphylococci: a state-of-the-art review.Acta veterinaria Scandinavica · 2024Review
- Development of a novel endolysin, PanLys.1, for the specific inhibition of Peptostreptococcus anaerobius.Animal bioscience · 2023Article
- Potential Role of the Host-Derived Cell-Wall Binding Domain of Endolysin CD16/50L as a Molecular Anchor in Preservation of Uninfected Clostridioides difficile for New Rounds of Phage Infection.Microbiology spectrum · 2022Article
- Endolysins against Streptococci as an antibiotic alternative.Frontiers in microbiology · 2022Review
- Direct Lytic Agents: Novel, Rapidly Acting Potential Antimicrobial Treatment Modalities for Systemic Use in the Era of Rising Antibiotic Resistance.Frontiers in microbiology · 2022Review
- Structural and biochemical analyses of the tetrameric cell binding domain of Lys170 from enterococcal phage F170/08.European biophysics journal : EBJ · 2021Article
- Sequence-Function Relationships in Phage-Encoded Bacterial Cell Wall Lytic Enzymes and Their Implications for Phage-Derived Product Design.Journal of virology · 2021Article
- Structural and Functional Insights Into Skl and Pal Endolysins, Two Cysteine-Amidases With Anti-pneumococcal Activity. Dithiothreitol (DTT) Effect on Lytic Activity.Frontiers in microbiology · 2021Article
- A New Phage Lysin Isolated from the Oral Microbiome TargetingPharmaceuticals (Basel, Switzerland) · 2020Article
- Structural basis for recognition of bacterial cell wall teichoic acid by pseudo-symmetric SH3b-like repeats of a viral peptidoglycan hydrolase.Chemical science · 2020Article
- Structural and functional insights into a novel two-component endolysin encoded by a single gene in Enterococcus faecalis phage.PLoS pathogens · 2020Article
- Production of bacteriophage-encoded endolysin, LysP11, in Nicotiana benthamiana and its activity as a potent antimicrobial agent against Erysipelothrix rhusiopathiae.Plant cell reports · 2019Article
- Microarray Strategies for Exploring Bacterial Surface Glycans and Their Interactions With Glycan-Binding Proteins.Frontiers in microbiology · 2019Review
- Phage Lysins for Fighting Bacterial Respiratory Infections: A New Generation of Antimicrobials.Frontiers in immunology · 2018Review
Corrections and comments
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Authors and funding
13 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Endolysins, the cell wall lytic enzymes encoded by bacteriophages to release the phage progeny, are among the top alternatives to fight against multiresistant pathogenic bacteria; one of the current biggest challenges to global health. Their narrow range of susceptible bacteria relies, primarily, on targeting specific cell-wall receptors through specialized modules. The cell wall-binding domain of Cpl-7 endolysin, made of three CW_7 repeats, accounts for its extended-range of substrates. Using as model system the cell wall-binding domain of Cpl-7, here we describe the molecular basis for the bacterial cell wall recognition by the CW_7 motif, which is widely represented in sequences of cell wall hydrolases. We report the crystal and solution structure of the full-length domain, identify N-acetyl-D-glucosaminyl-(β1,4)-N-acetylmuramyl-L-alanyl-D-isoglutamine (GMDP) as the peptidoglycan (PG) target recognized by the CW_7 motifs, and characterize feasible GMDP-CW_7 contacts. Our data suggest that Cpl-7 cell wall-binding domain might simultaneously bind to three PG chains, and also highlight the potential use of CW_7-containing lysins as novel anti-infectives.
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