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Pharmaceuticals 2018, 11(1), 25; https://doi.org/10.3390/ph11010025

Characterization of the Lytic Capability of a LysK-Like Endolysin, Lys-phiSA012, Derived from a Polyvalent Staphylococcus aureus Bacteriophage

1
Laboratory of Biochemistry, School of Veterinary Medicine, Rakuno Gakuen University, Ebetsu 069-8501, Japan
2
Laboratory of Food Microbiology and Food Safety, School of Veterinary Medicine, Rakuno Gakuen University, Ebetsu 069-8501, Japan
3
Laboratory of Veterinary Hygiene, School of Veterinary Medicine, Rakuno Gakuen University, Ebetsu 069-8501, Japan
4
Department of Bioengineering, Tokyo Institute of Technology, Yokohama 226-8502, Japan
5
Center for Veterinary Drug Development, Rakuno Gakuen University, Ebetsu 069-8501, Japan
These authors contributed equally to this paper.
*
Author to whom correspondence should be addressed.
Received: 4 January 2018 / Revised: 17 February 2018 / Accepted: 19 February 2018 / Published: 24 February 2018
(This article belongs to the Special Issue Phage Therapy and Phage-Mediated Biological Control)
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Abstract

Antibiotic-resistant bacteria (ARB) have spread widely and rapidly, with their increased occurrence corresponding with the increased use of antibiotics. Infections caused by Staphylococcus aureus have a considerable negative impact on human and livestock health. Bacteriophages and their peptidoglycan hydrolytic enzymes (endolysins) have received significant attention as novel approaches against ARB, including S. aureus. In the present study, we purified an endolysin, Lys-phiSA012, which harbors a cysteine/histidine-dependent amidohydrolase/peptidase (CHAP) domain, an amidase domain, and a SH3b cell wall binding domain, derived from a polyvalent S. aureus bacteriophage which we reported previously. We demonstrate that Lys-phiSA012 exhibits high lytic activity towards staphylococcal strains, including methicillin-resistant S. aureus (MRSA). Analysis of deletion mutants showed that only mutants possessing the CHAP and SH3b domains could lyse S. aureus, indicating that lytic activity of the CHAP domain depended on the SH3b domain. The presence of at least 1 mM Ca2+ and 100 µM Zn2+ enhanced the lytic activity of Lys-phiSA012 in a turbidity reduction assay. Furthermore, a minimum inhibitory concentration (MIC) assay showed that the addition of Lys-phiSA012 decreased the MIC of oxacillin. Our results suggest that endolysins are a promising approach for replacing current antimicrobial agents and may contribute to the proper use of antibiotics, leading to the reduction of ARB. View Full-Text
Keywords: antibiotic resistant; multidrug resistant; antimicrobial agent; phage therapy; bacteriophage; endolysin; staphylococci; Staphylococcus aureus antibiotic resistant; multidrug resistant; antimicrobial agent; phage therapy; bacteriophage; endolysin; staphylococci; Staphylococcus aureus
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Fujiki, J.; Nakamura, T.; Furusawa, T.; Ohno, H.; Takahashi, H.; Kitana, J.; Usui, M.; Higuchi, H.; Tanji, Y.; Tamura, Y.; Iwano, H. Characterization of the Lytic Capability of a LysK-Like Endolysin, Lys-phiSA012, Derived from a Polyvalent Staphylococcus aureus Bacteriophage. Pharmaceuticals 2018, 11, 25.

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