Evidence map›Paper›PMID 25630640›Full record

ArticleThe Journal of antimicrobial chemotherapy2015

Evolutionarily distinct bacteriophage endolysins featuring conserved peptidoglycan cleavage sites protect mice from MRSA infection.

Mathias Schmelcher, Yang Shen, Daniel C Nelson, Marcel R Eugster, Fritz Eichenseher, Daniela C Hanke, Martin J Loessner, Shengli Dong, David G Pritchard, Jean C Lee and 3 more

Open access · greenAbstract read
In one paragraph

Article in The Journal of antimicrobial chemotherapy, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
14.0field-weighted citation impact, top 1% 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

83 citing papers in PubMed, 142 citations in OpenAlex.

  1. Review
  2. Gut virome dynamics: from commensal to critical player in health and disease.Nature reviews. Gastroenterology & hepatology · 2026
    Review
  3. Article
  4. Recent Advances in Endolysin Engineering.Antibiotics (Basel, Switzerland) · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. [Phage endolysins-a novel class of antibacterial agents with a wide range of applications].Bundesgesundheitsblatt, Gesundheitsforschung, Gesundheitsschutz · 2025
    Review
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  11. Article
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23 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 5 institutions in 2 countries.

Mathias SchmelcherAnimal Biosciences and Biotechnology Laboratory, ANRI, NEA, ARS, USDA, 10300 Baltimore Ave., Beltsville, MD 20705-2350, USA Institute of Food, Nutrition and Health, ETH Zurich, Schmelzbergstrasse 7, 8092 Zurich, Switzerland mathias.schmelcher@hest.ethz.ch.
Yang ShenInstitute of Food, Nutrition and Health, ETH Zurich, Schmelzbergstrasse 7, 8092 Zurich, Switzerland Institute for Bioscience and Biotechnology Research, University of Maryland, 9600 Gudelsky Drive, Rockville, MD 20850, USA.
Daniel C NelsonInstitute for Bioscience and Biotechnology Research, University of Maryland, 9600 Gudelsky Drive, Rockville, MD 20850, USA Department of Veterinary Medicine, University of Maryland, 8075 Greenmead Drive, College Park, MD 20742, USA.
Marcel R EugsterInstitute of Food, Nutrition and Health, ETH Zurich, Schmelzbergstrasse 7, 8092 Zurich, Switzerland.
Fritz EichenseherInstitute of Food, Nutrition and Health, ETH Zurich, Schmelzbergstrasse 7, 8092 Zurich, Switzerland.
Daniela C HankeInstitute of Food, Nutrition and Health, ETH Zurich, Schmelzbergstrasse 7, 8092 Zurich, Switzerland.
Martin J LoessnerInstitute of Food, Nutrition and Health, ETH Zurich, Schmelzbergstrasse 7, 8092 Zurich, Switzerland.
Shengli DongDepartment of Biochemistry and Molecular Genetics, MCLM 552, University of Alabama at Birmingham, 1530 3rd Ave., Birmingham, AL 35294-0005, USA.
David G PritchardDepartment of Biochemistry and Molecular Genetics, MCLM 552, University of Alabama at Birmingham, 1530 3rd Ave., Birmingham, AL 35294-0005, USA.
Jean C LeeChanning Laboratory, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA.
Stephen C BeckerAnimal Biosciences and Biotechnology Laboratory, ANRI, NEA, ARS, USDA, 10300 Baltimore Ave., Beltsville, MD 20705-2350, USA.
Juli Foster-FreyAnimal Biosciences and Biotechnology Laboratory, ANRI, NEA, ARS, USDA, 10300 Baltimore Ave., Beltsville, MD 20705-2350, USA.
David M DonovanAnimal Biosciences and Biotechnology Laboratory, ANRI, NEA, ARS, USDA, 10300 Baltimore Ave., Beltsville, MD 20705-2350, USA.
ETH Zurich · CHUniversity of Alabama at Birmingham · USHarvard University · USInstitute for Bioscience and Biotechnology ResearchUniversity of Maryland, College Park · US

Funding

Triple action chimera: eradication of nasal S. aureus by cell wall hydrolasesR01AI075077 · NIAID · U.S. AGRICULTURAL RESEARCH CENTER · PI DONOVAN, DAVID MATTHEW · 2008 to 2010
$697k
NIAID NIH HHS 1R01AI075077-01A1NIAID NIH HHS HHSN272200700055C
6 · The paper itself

Abstract

objectivesIn the light of increasing drug resistance in Staphylococcus aureus, bacteriophage endolysins [peptidoglycan hydrolases (PGHs)] have been suggested as promising antimicrobial agents. The aim of this study was to determine the antimicrobial activity of nine enzymes representing unique homology groups within a diverse class of staphylococcal PGHs.

methodsPGHs were recombinantly expressed, purified and tested for staphylolytic activity in multiple in vitro assays (zymogram, turbidity reduction assay and plate lysis) and against a comprehensive set of strains (S. aureus and CoNS). PGH cut sites in the staphylococcal peptidoglycan were determined by biochemical assays (Park-Johnson and Ghuysen procedures) and MS analysis. The enzymes were tested for their ability to eradicate static S. aureus biofilms and compared for their efficacy against systemic MRSA infection in a mouse model.

resultsDespite similar modular architectures and unexpectedly conserved cleavage sites in the peptidoglycan (conferred by evolutionarily divergent catalytic domains), the enzymes displayed varying degrees of in vitro lytic activity against numerous staphylococcal strains, including cell surface mutants and drug-resistant strains, and proved effective against static biofilms. In a mouse model of systemic MRSA infection, six PGHs provided 100% protection from death, with animals being free of clinical signs at the end of the experiment.

conclusionsOur results corroborate the high potential of PGHs for treatment of S. aureus infections and reveal unique antimicrobial and biochemical properties of the different enzymes, suggesting a high diversity of potential applications despite highly conserved peptidoglycan target sites.

Indexed as

AnimalsAnti-Bacterial AgentsBacteremiaBacteriophagesBiological TherapyCell WallDisease Models, AnimalEndopeptidasesFemaleHydrolysisMethicillin-Resistant Staphylococcus aureusMice, Inbred BALB CMicrobial Sensitivity TestsPeptidoglycanRecombinant ProteinsStaphylococcal InfectionsAnti-Bacterial AgentsendolysinEndopeptidasesPeptidoglycanRecombinant Proteinsantibiotic resistanceantimicrobialbiofilmpeptidoglycan hydrolase

Identifiers

PMID25630640
PMCPMC4398471
OpenAlexW1985226473

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.