Evidence map›Paper›PMID 29495476›Full record

ReviewAntibiotics (Basel, Switzerland)2018

Potential for Bacteriophage Endolysins to Supplement or Replace Antibiotics in Food Production and Clinical Care.

Michael J Love, Dinesh Bhandari, Renwick C J Dobson, Craig Billington

Open access · goldAbstract readReview
In one paragraph

Review in Antibiotics (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
18.3field-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

79 citing papers in PubMed, 175 citations in OpenAlex.

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  20. Characterization and Engineering Studies of a New Endolysin from theInternational journal of molecular sciences · 2023
    Article

19 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

4 authors at 2 institutions in 2 countries.

Michael J LoveBiomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, Christchurch 8041, New Zealand. michael.love@pg.canterbury.ac.nz.
Dinesh BhandariBiomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, Christchurch 8041, New Zealand. dinesh.bhandari@esr.cri.nz.
Renwick C J DobsonBiomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, Christchurch 8041, New Zealand. renwick.dobson@canterbury.ac.nz.
Craig BillingtonBiomolecular Interaction Centre and School of Biological Sciences, University of Canterbury, Christchurch 8041, New Zealand. craig.billington@esr.cri.nz.ORCID 0000-0003-3433-4220
University of Canterbury · NZThe University of Melbourne · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There is growing concern about the emergence of bacterial strains showing resistance to all classes of antibiotics commonly used in human medicine. Despite the broad range of available antibiotics, bacterial resistance has been identified for every antimicrobial drug developed to date. Alarmingly, there is also an increasing prevalence of multidrug-resistant bacterial strains, rendering some patients effectively untreatable. Therefore, there is an urgent need to develop alternatives to conventional antibiotics for use in the treatment of both humans and food-producing animals. Bacteriophage-encoded lytic enzymes (endolysins), which degrade the cell wall of the bacterial host to release progeny virions, are potential alternatives to antibiotics. Preliminary studies show that endolysins can disrupt the cell wall when applied exogenously, though this has so far proven more effective in Gram-positive bacteria compared with Gram-negative bacteria. Their potential for development is furthered by the prospect of bioengineering, and aided by the modular domain structure of many endolysins, which separates the binding and catalytic activities into distinct subunits. These subunits can be rearranged to create novel, chimeric enzymes with optimized functionality. Furthermore, there is evidence that the development of resistance to these enzymes may be more difficult compared with conventional antibiotics due to their targeting of highly conserved bonds.

Indexed as

antibioticsantimicrobial resistanceendolysinone healthprotein engineering

Identifiers

PMID29495476
PMCPMC5872128
OpenAlexW2395104290

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.