Novel Phage-Derived Depolymerase with Activity against Proteus mirabilis Biofilms.

Area of Science:

• Microbiology and Infectious Diseases
• Bacteriophage Therapy
• Biofilm Research

Background:

• Proteus mirabilis forms crystalline biofilms on urinary catheters, causing infections and antibiotic resistance.
• Current antibiotic treatments are often ineffective against these biofilms.
• Bacteriophages and their enzymes are emerging as alternative therapeutic strategies.

Purpose of the Study:

• To isolate and characterize a novel Proteus bacteriophage.
• To investigate the biofilm degradation potential of a specific phage enzyme.
• To evaluate the therapeutic efficacy of this enzyme against Proteus infections.

Main Methods:

• Isolation and full characterization of a novel Proteus bacteriophage (vB_PmiS_PM-CJR).
• Genome analysis to identify a pectate lyase domain in the tail spike protein.
• Heterologous expression and purification of the tail spike protein.
• Testing biofilm degradation using MBEC assays and Galleria mellonella infection models.

Main Results:

• The isolated phage exhibited depolymerase activity.
• The purified tail spike protein significantly reduced Proteus biofilm adherence to plastic.
• Application of the tail spike protein improved survival rates in infected Galleria mellonella larvae.

Conclusions:

• This study is the first to isolate and characterize a biofilm depolymerase from a Proteus phage.
• The phage tail spike protein demonstrates significant potential for degrading Proteus biofilms.
• This enzyme represents a promising new avenue for treating Proteus-associated infections and combating antibiotic resistance.