ArticleThe Journal of biological chemistry2010
Cpl-7, a lysozyme encoded by a pneumococcal bacteriophage with a novel cell wall-binding motif.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 46 citations in OpenAlex.
- Bacterial meningitis in adults: therapeutic challenges in the era of antibiotic resistance and the potential of bacteriophages and associated by products.Frontiers in cellular and infection microbiology · 2026Review
- Novel endolysin fromJournal of microbiology and biotechnology · 2025Article
- Development of a novel endolysin, PanLys.1, for the specific inhibition of Peptostreptococcus anaerobius.Animal bioscience · 2023Article
- Therapeutic potential of bacteriophage endolysins for infections caused by Gram-positive bacteria.Journal of biomedical science · 2023Review
- Lysozyme and Its Application as Antibacterial Agent in Food Industry.Molecules (Basel, Switzerland) · 2022Review
- Endolysins against Streptococci as an antibiotic alternative.Frontiers in microbiology · 2022Review
- Gram-Positive Pneumonia: Possibilities Offered by Phage Therapy.Antibiotics (Basel, Switzerland) · 2021Review
- Article
- Phage-Encoded Endolysins.Antibiotics (Basel, Switzerland) · 2021Review
- A New Phage Lysin Isolated from the Oral Microbiome TargetingPharmaceuticals (Basel, Switzerland) · 2020Article
- Characterization of MSlys, the endolysin ofBiotechnology reports (Amsterdam, Netherlands) · 2020Article
- A Choline-Recognizing Monomeric Lysin, ClyJ-3m, Shows Elevated Activity against Streptococcus pneumoniae.Antimicrobial agents and chemotherapy · 2020Article
- Linker Editing of Pneumococcal Lysin ClyJ Conveys Improved Bactericidal Activity.Antimicrobial agents and chemotherapy · 2020Article
- ClyJ Is a Novel Pneumococcal Chimeric Lysin with a Cysteine- and Histidine-Dependent Amidohydrolase/Peptidase Catalytic Domain.Antimicrobial agents and chemotherapy · 2019Article
- Synergy Between Two Chimeric Lysins to KillFrontiers in microbiology · 2019Article
- Bactericidal synergism between antibiotics and phage endolysin Cpl-711 to kill multidrug-resistant pneumococcus.Future microbiology · 2018Article
- Phage Lysins for Fighting Bacterial Respiratory Infections: A New Generation of Antimicrobials.Frontiers in immunology · 2018Review
- Surfaceome and Proteosurfaceome in Parietal Monoderm Bacteria: Focus on Protein Cell-Surface Display.Frontiers in microbiology · 2018Review
- Deciphering how Cpl-7 cell wall-binding repeats recognize the bacterial peptidoglycan.Scientific reports · 2017Article
- Csl2, a novel chimeric bacteriophage lysin to fight infections caused by Streptococcus suis, an emerging zoonotic pathogen.Scientific reports · 2017Article
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Authors and funding
10 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteriophage endolysins include a group of new antibacterials reluctant to development of resistance. We present here the first structural study of the Cpl-7 endolysin, encoded by pneumococcal bacteriophage Cp-7. It contains an N-terminal catalytic module (CM) belonging to the GH25 family of glycosyl hydrolases and a C-terminal region encompassing three identical repeats of 42 amino acids (CW_7 repeats). These repeats are unrelated to choline-targeting motifs present in other cell wall hydrolases produced by Streptococcus pneumoniae and its bacteriophages, and are responsible for the protein attachment to the cell wall. By combining different biophysical techniques and molecular modeling, a three-dimensional model of the overall protein structure is proposed, consistent with circular dichroism and sequence-based secondary structure prediction, small angle x-ray scattering data, and Cpl-7 hydrodynamic behavior. Cpl-7 is an ∼115-Å long molecule with two well differentiated regions, corresponding to the CM and the cell wall binding region (CWBR), arranged in a lateral disposition. The CM displays the (βα)(5)β(3) barrel topology characteristic of the GH25 family, and the impact of sequence differences with the CM of the Cpl-1 lysozyme in substrate binding is discussed. The CWBR is organized in three tandemly assembled three-helical bundles whose dispositions remind us of a super-helical structure. Its approximate dimensions are 60 × 20 × 20 Å and presents a concave face that might constitute the functional region involved in bacterial surface recognition. The distribution of CW_7 repeats in the sequences deposited in the Entrez Database have been examined, and the results drastically expanded the antimicrobial potential of the Cpl-7 endolysin.
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