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The efficacy of lyticase and β-glucosidase enzymes on biofilm degradation of Pseudomonas aeruginosa strains with different gene profiles

BACKGROUND: Pseudomonas aeruginosa is a nosocomial pathogen that causes severe infections in immunocompromised patients. Biofilm plays a significant role in the resistance of this bacterium and complicates the treatment of its infections. In this study, the effect of lyticase and β-glucosidase enzym...

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Autores principales: Banar, Maryam, Emaneini, Mohammad, Beigverdi, Reza, Fanaei Pirlar, Rima, Node Farahani, Narges, van Leeuwen, Willem B., Jabalameli, Fereshteh
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6909625/
https://www.ncbi.nlm.nih.gov/pubmed/31830915
http://dx.doi.org/10.1186/s12866-019-1662-9
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author Banar, Maryam
Emaneini, Mohammad
Beigverdi, Reza
Fanaei Pirlar, Rima
Node Farahani, Narges
van Leeuwen, Willem B.
Jabalameli, Fereshteh
author_facet Banar, Maryam
Emaneini, Mohammad
Beigverdi, Reza
Fanaei Pirlar, Rima
Node Farahani, Narges
van Leeuwen, Willem B.
Jabalameli, Fereshteh
author_sort Banar, Maryam
collection PubMed
description BACKGROUND: Pseudomonas aeruginosa is a nosocomial pathogen that causes severe infections in immunocompromised patients. Biofilm plays a significant role in the resistance of this bacterium and complicates the treatment of its infections. In this study, the effect of lyticase and β-glucosidase enzymes on the degradation of biofilms of P. aeruginosa strains isolated from cystic fibrosis and burn wound infections were assessed. Moreover, the decrease of ceftazidime minimum biofilm eliminating concentrations (MBEC) after enzymatic treatment was evaluated. RESULTS: This study demonstrated the effectiveness of both enzymes in degrading the biofilms of P. aeruginosa. In contrast to the lyticase enzyme, β-glucosidase reduced the ceftazidime MBECs significantly (P < 0.05). Both enzymes had no cytotoxic effect on the A-549 human lung carcinoma epithelial cell lines and A-431 human epidermoid carcinoma cell lines. CONCLUSION: Considering the characteristics of the β-glucosidase enzyme, which includes the notable degradation of P. aeruginosa biofilms and a significant decrease in the ceftazidime MBECs and non-toxicity for eukaryotic cells, this enzyme can be a promising therapeutic candidate for degradation of biofilms in burn wound patients, but further studies are needed.
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spelling pubmed-69096252019-12-30 The efficacy of lyticase and β-glucosidase enzymes on biofilm degradation of Pseudomonas aeruginosa strains with different gene profiles Banar, Maryam Emaneini, Mohammad Beigverdi, Reza Fanaei Pirlar, Rima Node Farahani, Narges van Leeuwen, Willem B. Jabalameli, Fereshteh BMC Microbiol Research Article BACKGROUND: Pseudomonas aeruginosa is a nosocomial pathogen that causes severe infections in immunocompromised patients. Biofilm plays a significant role in the resistance of this bacterium and complicates the treatment of its infections. In this study, the effect of lyticase and β-glucosidase enzymes on the degradation of biofilms of P. aeruginosa strains isolated from cystic fibrosis and burn wound infections were assessed. Moreover, the decrease of ceftazidime minimum biofilm eliminating concentrations (MBEC) after enzymatic treatment was evaluated. RESULTS: This study demonstrated the effectiveness of both enzymes in degrading the biofilms of P. aeruginosa. In contrast to the lyticase enzyme, β-glucosidase reduced the ceftazidime MBECs significantly (P < 0.05). Both enzymes had no cytotoxic effect on the A-549 human lung carcinoma epithelial cell lines and A-431 human epidermoid carcinoma cell lines. CONCLUSION: Considering the characteristics of the β-glucosidase enzyme, which includes the notable degradation of P. aeruginosa biofilms and a significant decrease in the ceftazidime MBECs and non-toxicity for eukaryotic cells, this enzyme can be a promising therapeutic candidate for degradation of biofilms in burn wound patients, but further studies are needed. BioMed Central 2019-12-12 /pmc/articles/PMC6909625/ /pubmed/31830915 http://dx.doi.org/10.1186/s12866-019-1662-9 Text en © The Author(s). 2019 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research Article
Banar, Maryam
Emaneini, Mohammad
Beigverdi, Reza
Fanaei Pirlar, Rima
Node Farahani, Narges
van Leeuwen, Willem B.
Jabalameli, Fereshteh
The efficacy of lyticase and β-glucosidase enzymes on biofilm degradation of Pseudomonas aeruginosa strains with different gene profiles
title The efficacy of lyticase and β-glucosidase enzymes on biofilm degradation of Pseudomonas aeruginosa strains with different gene profiles
title_full The efficacy of lyticase and β-glucosidase enzymes on biofilm degradation of Pseudomonas aeruginosa strains with different gene profiles
title_fullStr The efficacy of lyticase and β-glucosidase enzymes on biofilm degradation of Pseudomonas aeruginosa strains with different gene profiles
title_full_unstemmed The efficacy of lyticase and β-glucosidase enzymes on biofilm degradation of Pseudomonas aeruginosa strains with different gene profiles
title_short The efficacy of lyticase and β-glucosidase enzymes on biofilm degradation of Pseudomonas aeruginosa strains with different gene profiles
title_sort efficacy of lyticase and β-glucosidase enzymes on biofilm degradation of pseudomonas aeruginosa strains with different gene profiles
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6909625/
https://www.ncbi.nlm.nih.gov/pubmed/31830915
http://dx.doi.org/10.1186/s12866-019-1662-9
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