Next Article in Journal
Genome Analysis of A Novel South African Cydia pomonella granulovirus (CpGV-SA) with Resistance-Breaking Potential
Next Article in Special Issue
Lyophilized Matrix Containing Ready-to-Use Primers and Probe Solution for Standardization of Real-Time PCR and RT-qPCR Diagnostics in Virology
Previous Article in Journal
Human Virome and Disease: High-Throughput Sequencing for Virus Discovery, Identification of Phage-Bacteria Dysbiosis and Development of Therapeutic Approaches with Emphasis on the Human Gut
Article

Ts2631 Endolysin from the Extremophilic Thermus scotoductus Bacteriophage vB_Tsc2631 as an Antimicrobial Agent against Gram-Negative Multidrug-Resistant Bacteria

1
Laboratory of Extremophiles Biology, Department of Microbiology, Faculty of Biology, University of Gdansk, 80-822 Gdansk, Poland
2
Department of Plant Cytology and Embryology, Faculty of Biology, University of Gdansk, 80-308 Gdansk, Poland
3
Collection of Plasmids and Microorganisms, Faculty of Biology, University of Gdansk, 80-308 Gdansk, Poland
*
Authors to whom correspondence should be addressed.
Viruses 2019, 11(7), 657; https://doi.org/10.3390/v11070657
Received: 5 June 2019 / Revised: 12 July 2019 / Accepted: 15 July 2019 / Published: 18 July 2019
(This article belongs to the Special Issue Novel Concepts in Virology)
Bacteria that thrive in extreme conditions and the bacteriophages that infect them are sources of valuable enzymes resistant to denaturation at high temperatures. Many of these heat-stable proteins are useful for biotechnological applications; nevertheless, none have been utilized as antibacterial agents. Here, we demonstrate the bactericidal potential of Ts2631 endolysin from the extremophilic bacteriophage vB_Tsc2631, which infects Thermus scotoductus, against the alarming multidrug-resistant clinical strains of Acinetobacter baumannii, Pseudomonas aeruginosa and pathogens from the Enterobacteriaceae family. A 2–3.7 log reduction in the bacterial load was observed in antibacterial tests against A. baumannii and P. aeruginosa after 1.5 h. The Ts2631 activity was further enhanced by ethylenediaminetetraacetic acid (EDTA), a metal ion chelator (4.2 log reduction in carbapenem-resistant A. baumannii) and, to a lesser extent, by malic acid and citric acid (2.9 and 3.3 log reductions, respectively). The EDTA/Ts2631 combination reduced all pathogens of the Enterobacteriaceae family, particularly multidrug-resistant Citrobacter braakii, to levels below the detection limit (>6 log); these results indicate that Ts2631 endolysin could be useful to combat Gram-negative pathogens. The investigation of A. baumannii cells treated with Ts2631 endolysin variants under transmission electron and fluorescence microscopy demonstrates that the intrinsic antibacterial activity of Ts2631 endolysin is dependent on the presence of its N-terminal tail. View Full-Text
Keywords: lytic enzyme; Peptidoglycan recognition proteins (PGRPs); peptidoglycan; Pseudomonas aeruginosa; Acinetobacter baumannii lytic enzyme; Peptidoglycan recognition proteins (PGRPs); peptidoglycan; Pseudomonas aeruginosa; Acinetobacter baumannii
Show Figures

Figure 1

MDPI and ACS Style

Plotka, M.; Kapusta, M.; Dorawa, S.; Kaczorowska, A.-K.; Kaczorowski, T. Ts2631 Endolysin from the Extremophilic Thermus scotoductus Bacteriophage vB_Tsc2631 as an Antimicrobial Agent against Gram-Negative Multidrug-Resistant Bacteria. Viruses 2019, 11, 657. https://doi.org/10.3390/v11070657

AMA Style

Plotka M, Kapusta M, Dorawa S, Kaczorowska A-K, Kaczorowski T. Ts2631 Endolysin from the Extremophilic Thermus scotoductus Bacteriophage vB_Tsc2631 as an Antimicrobial Agent against Gram-Negative Multidrug-Resistant Bacteria. Viruses. 2019; 11(7):657. https://doi.org/10.3390/v11070657

Chicago/Turabian Style

Plotka, Magdalena; Kapusta, Malgorzata; Dorawa, Sebastian; Kaczorowska, Anna-Karina; Kaczorowski, Tadeusz. 2019. "Ts2631 Endolysin from the Extremophilic Thermus scotoductus Bacteriophage vB_Tsc2631 as an Antimicrobial Agent against Gram-Negative Multidrug-Resistant Bacteria" Viruses 11, no. 7: 657. https://doi.org/10.3390/v11070657

Find Other Styles
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop