Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/123843
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Type: Journal article
Title: Potential for bacteriophage endolysins to supplement or replace antibiotics in food production and clinical care
Author: Love, M.
Bhandari, D.
Dobson, R.
Billington, C.
Citation: Antibiotics, 2018; 7(1):17-1-17-25
Publisher: MDPI AG
Issue Date: 2018
ISSN: 2079-6382
2079-6382
Statement of
Responsibility: 
Michael J. Love, Dinesh Bhandari, Renwick C. J. Dobson and Craig Billington
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.
Keywords: endolysin; antibiotics; antimicrobial resistance; one health; protein engineering
Description: Published: 27 February 2018
Rights: © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
RMID: 0030085888
DOI: 10.3390/antibiotics7010017
Appears in Collections:Public Health publications

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