Bacteriophage φEf11 ORF28 Endolysin, a Multifunctional Lytic Enzyme with Properties Distinct from All Other Identified Enterococcus faecalis Phage Endolysins

Author:

Zhang Hongming12,Buttaro Bettina A.3,Fouts Derrick E.4ORCID,Sanjari Salar1,Evans Bradley S.5,Stevens Roy H.123

Affiliation:

1. Department of Endodontology, Kornberg School of Dentistry, Temple University, Philadelphia, Pennsylvania, USA

2. Laboratory of Oral Infectious Diseases, Kornberg School of Dentistry, Temple University, Philadelphia, Pennsylvania, USA

3. Department of Microbiology & Immunology, Katz School of Medicine, Temple University, Philadelphia, Pennsylvania, USA

4. Infectious Diseases, J. Craig Venter Institute, Rockville, Maryland, USA

5. Proteomics & Mass Spectrometry CORE, Danforth Plant Science Center, St. Louis, Missouri, USA

Abstract

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 of Enterococcus faecalis . The lysin is broadly active against most of the tested E. faecalis strains and exhibits multifunctional enzymatic specificities that differ from all other characterized endolysins produced by E. faecalis bacteriophages.

Funder

HHS | National Institutes of Health

J&J | Janssen Research and Development

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

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