Journal
MICROORGANISMS
Volume 9, Issue 10, Pages -Publisher
MDPI
DOI: 10.3390/microorganisms9102172
Keywords
Proteus; bacteriophage; urinary tract infections (UTIs); depolymerases; antibiotic resistance; pectate lyase; biofilms
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Funding
- Northern Ireland Department for the Economy (DfE)
- Wellcome Trust Biomedical Vacation Scholarship [216936/Z/19/Z]
- Cystic Fibrosis Trust and British Lung Foundation [SS19/08]
- Wellcome Trust [216936/Z/19/Z] Funding Source: Wellcome Trust
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Proteus mirabilis adheres to urinary catheters and forms biofilms, leading to blockage and decreased antibiotic effectiveness, potentially causing antibiotic resistance. Bacteriophages and their enzymes are being explored as alternative treatment options.
The adherence of Proteus mirabilis to the surface of urinary catheters leads to colonization and eventual blockage of the catheter lumen by unique crystalline biofilms produced by these opportunistic pathogens, making P. mirabilis one of the leading causes of catheter-associated urinary tract infections. The Proteus biofilms reduce efficiency of antibiotic-based treatment, which in turn increases the risk of antibiotic resistance development. Bacteriophages and their enzymes have recently become investigated as alternative treatment options. In this study, a novel Proteus bacteriophage (vB_PmiS_PM-CJR) was isolated from an environmental sample and fully characterized. The phage displayed depolymerase activity and the subsequent genome analysis revealed the presence of a pectate lyase domain in its tail spike protein. The protein was heterologously expressed and purified; the ability of the purified tail spike to degrade Proteus biofilms was tested. We showed that the application of the tail spike protein was able to reduce the adherence of bacterial biofilm to plastic pegs in a MBEC (minimum biofilm eradication concentration) assay and improve the survival of Galleria mellonella larvae infected with Proteus mirabilis. Our study is the first to successfully isolate and characterize a biofilm depolymerase from a Proteus phage, demonstrating the potential of this group of enzymes in treatment of Proteus infections.
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