ArticlePloS one2012
Thermal stability of Cpl-7 endolysin from the streptococcus pneumoniae bacteriophage Cp-7; cell wall-targeting of its CW_7 motifs.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- Identification of cell wall binding domains and repeats inBiochemistry and biophysics reports · 2024Article
- Article
- Metagenomic analysis of hot spring soil for mining a novel thermostable enzybiotic.Applied microbiology and biotechnology · 2024Article
- Endolysins against Streptococci as an antibiotic alternative.Frontiers in microbiology · 2022Review
- Enhancing Whole Phage Therapy and Their Derived Antimicrobial Enzymes through Complex Formulation.Pharmaceuticals (Basel, Switzerland) · 2018Review
- Surfaceome and Proteosurfaceome in Parietal Monoderm Bacteria: Focus on Protein Cell-Surface Display.Frontiers in microbiology · 2018Review
- Csl2, a novel chimeric bacteriophage lysin to fight infections caused by Streptococcus suis, an emerging zoonotic pathogen.Scientific reports · 2017Article
- Deciphering how Cpl-7 cell wall-binding repeats recognize the bacterial peptidoglycan.Scientific reports · 2017Article
- A chimeolysin with extended-spectrum streptococcal host range found by an induced lysis-based rapid screening method.Scientific reports · 2015Article
- Article
- Biochemical characterization of the major N-acetylmuramidase from Lactobacillus buchneri.Microbiology (Reading, England) · 2014Article
- Improving the lethal effect of cpl-7, a pneumococcal phage lysozyme with broad bactericidal activity, by inverting the net charge of its cell wall-binding module.Antimicrobial agents and chemotherapy · 2013Article
- A novel type of peptidoglycan-binding domain highly specific for amidated D-Asp cross-bridge, identified in Lactobacillus casei bacteriophage endolysins.The Journal of biological chemistry · 2013Article
- Enzymatic characterization of a lysin encoded by bacteriophage EL.Bacteriophage · 2013Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Endolysins comprise a novel class of selective antibacterials refractory to develop resistances. The Cpl-7 endolysin, encoded by the Streptococcus pneumoniae bacteriophage Cp-7, consists of a catalytic module (CM) with muramidase activity and a cell wall-binding module (CWBM) made of three fully conserved CW_7 repeats essential for activity. Firstly identified in the Cpl-7 endolysin, CW_7 motifs are also present in a great variety of cell wall hydrolases encoded, among others, by human and live-stock pathogens. However, the nature of CW_7 receptors on the bacterial envelope remains unknown. In the present study, the structural stability of Cpl-7 and the target recognized by CW_7 repeats, relevant for exploitation of Cpl-7 as antimicrobial, have been analyzed, and transitions from the CM and the CWBM assigned, using circular dichroism and differential scanning calorimetry. Cpl-7 stability is maximum around 6.0-6.5, near the optimal pH for activity. Above pH 8.0 the CM becomes extremely unstable, probably due to deprotonation of the N-terminal amino-group, whereas the CWBM is rather insensitive to pH variation and its structural stabilization by GlcNAc-MurNAc-l-Ala-d-isoGln points to the cell wall muropeptide as the cell wall target recognized by the CW_7 repeats. Denaturation data also revealed that Cpl-7 is organized into two essentially independent folding units, which will facilitate the recombination of the CM and the CWBM with other catalytic domains and/or cell wall-binding motifs to yield new tailored chimeric lysins with higher bactericidal activities or new pathogen specificities.
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