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Bacteriophage φEf11 ORF28 Endolysin, a Multifunctional Lytic Enzyme with Properties Distinct from All Other Identified Enterococcus faecalis Phage Endolysins
Author(s) -
Hongming Zhang,
Bettina A. Buttaro,
Derrick E. Fouts,
Salar Sanjari,
Bradley S. Evans,
Roy H. Stevens
Publication year - 2019
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.00555-19
Subject(s) - lysin , lytic cycle , bacteriophage , enterococcus faecalis , microbiology and biotechnology , biology , lysis , peptidoglycan , enterococcus , bacteria , enzyme , escherichia coli , virology , antibiotics , biochemistry , genetics , virus , staphylococcus aureus , gene
The emergence of multidrug-resistant pathogenic microorganisms has brought increasing attention to the urgent need for the development of alternative antimicrobial strategies. One such alternative to conventional antibiotics employs lytic enzymes (endolysins) that are produced by bacteriophages in the course of lytic infection. During lytic infection by a bacteriophage, these enzymes hydrolyze the cell wall peptidoglycan, resulting in the lysis of the host cell. However, external endolysin application can result in lysis from without. In this study, we have cloned, expressed, purified, and characterized an endolysin produced by a bacteriophage infecting strains ofEnterococcus faecalis . The lysin is broadly active against most of the testedE. faecalis strains and exhibits multifunctional enzymatic specificities that differ from all other characterized endolysins produced byE. faecalis bacteriophages.

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