Evidence map›Paper›PMID 23959317›Full record

ArticleAntimicrobial agents and chemotherapy2013

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.

Roberto Díez-Martínez, Héctor D de Paz, Héctor de Paz, Noemí Bustamante, Ernesto García, Margarita Menéndez, Pedro García

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
7.7field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

66 citing papers in PubMed, 108 citations in OpenAlex.

  1. Review
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  10. Endolysins: targetingFrontiers in microbiology · 2025
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6 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
    de Paz, Héctor [corrected to de Paz, Héctor D]
5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Roberto Díez-MartínezDepartamento de Microbiología Molecular y Biología de las Infecciones, Centro de Investigaciones Biológicas, CSIC, Madrid, Spain.
Héctor D de Paz
Héctor de Paz
Noemí Bustamante
Ernesto García
Margarita Menéndez
Pedro García
Centro de Investigación Biomédica en Red de Enfermedades Respiratorias · ESCentro de Investigaciones Biológicas Margarita Salas · ESInstituto de Química Física Blas Cabrera · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phage endolysins are murein hydrolases that break the bacterial cell wall to provoke lysis and release of phage progeny. Recently, these enzymes have also been recognized as powerful and specific antibacterial agents when added exogenously. In the pneumococcal system, most cell wall associated murein hydrolases reported so far depend on choline for activity, and Cpl-7 lysozyme constitutes a remarkable exception. Here, we report the improvement of the killing activity of the Cpl-7 endolysin by inversion of the sign of the charge of the cell wall-binding module (from -14.93 to +3.0 at neutral pH). The engineered variant, Cpl-7S, has 15 amino acid substitutions and an improved lytic activity against Streptococcus pneumoniae (including multiresistant strains), Streptococcus pyogenes, and other pathogens. Moreover, we have demonstrated that a single 25-μg dose of Cpl-7S significantly increased the survival rate of zebrafish embryos infected with S. pneumoniae or S. pyogenes, confirming the killing effect of Cpl-7S in vivo. Interestingly, Cpl-7S, in combination with 0.01% carvacrol (an essential oil), was also found to efficiently kill Gram-negative bacteria such as Escherichia coli and Pseudomonas putida, an effect not described previously. Our findings provide a strategy to improve the lytic activity of phage endolysins based on facilitating their pass through the negatively charged bacterial envelope, and thereby their interaction with the cell wall target, by modulating the net charge of the cell wall-binding modules.

Indexed as

Amino Acid SubstitutionAnimalsCell WallCholineCymenesEmbryo, NonmammalianEscherichia coliMonoterpenesMuramidaseProtein BindingProtein EngineeringPseudomonas putidaStatic ElectricityStreptococcus PhagesStreptococcus pneumoniaeStreptococcus pyogenescarvacrolCholineCPL7 lysozymeCymenesMonoterpenesMuramidaseViral Proteins

Identifiers

PMID23959317
PMCPMC3811316
OpenAlexW2096326200

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.