Abstract

BackgroundPseudomonas 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.ResultsThis 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.ConclusionConsidering 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.

Highlights

  • Pseudomonas aeruginosa is a nosocomial pathogen that causes severe infections in immunocompromised patients

  • Among the 122 P. aeruginosa clinical strains isolated from independent patients with cystic fibrosis (CF) or burn wound infections, a total of 11 strains were selected based on their unique gene profiles and phenotypic traits (Table 1)

  • The results demonstrated that both lyticase and β-glucosidase enzymes degraded the biofilms of P. aeruginosa strains with various gene profiles, altered the state of biofilms, and decreased the colony-forming units (CFU) significantly

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Summary

Introduction

Pseudomonas aeruginosa is a nosocomial pathogen that causes severe infections in immunocompromised patients. Pseudomonas aeruginosa is a nosocomial pathogen that causes severe infections in patients with cancer, cystic fibrosis (CF), and burn injuries [1, 2]. It accounts for about 10% of nosocomial infections [3]. The pslD gene encodes for a periplasmic protein that mediates the transmission of Psl polymer across the periplasmic space. Mutations in this gene result in a defect in Psl production [9]. The pelF gene encodes a cytoplasmic protein that is a glycosyltransferase and involves the transmission of sugar units of Pel as well as the Pel polymerization [13]

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