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Phage-Encoded Antimicrobial Peptide gp28 Demonstrates LL-37-Like Antimicrobial Activity Against Multidrug-Resistant
Rachael C Wilkinson1, Nerissa E Thomas1, Amita Bhatti1
1Swansea University Medical School, Healthcare Technology Centre, Swansea University, Swansea, United Kingdom.
Background:
Pseudomonas aeruginosa (P. aeruginosa) is a gram-negative bacterial pathogen commonly associated with nosocomial infections. Treatment of P. aeruginosa infections is notoriously difficult due to biofilm formation and antibiotic resistance. Antimicrobial peptides (AMPs) are thought to be promising new antimicrobials. Gp28, a phage-derived AMP, is a novel class of characterized phage AMPs with activity against Escherichia coli in a manner similar to the human peptide LL-37. LL-37 exhibits strong antimicrobial activity against P. aeruginosa as well as biofilm disruption and synergy with certain antibiotics posing the question whether gp28 could act similarly.
Methods:
Antibacterial activity of gp28 against P. aeruginosa was established using growth inhibition assays, with minimum inhibitory concentration calculated. Biofilm disruption was assessed using crystal violet staining and scanning electron microscopy. Combined treatment of gp28 with tobramycin against P. aeruginosa was measured using a modified time-kill assay at sublethal concentrations.
Results:
Gp28 inhibits P. aeruginosa planktonic growth, with a minimum inhibitory concentration of 109 μg mL-1 and disrupts established biofilms. We demonstrate that gp28 increases the susceptibility of P. aeruginosa to tobramycin.
Conclusions:
Gp28 demonstrates potential for development as a putative therapeutic agent against a clinically resistant P. aeruginosa strain either alone or in combination with the frontline antibiotic tobramycin.
Insights
The novel antimicrobial peptide gp28 effectively inhibits Pseudomonas aeruginosa growth and disrupts biofilms. Gp28 also enhances tobramycin efficacy, showing potential against antibiotic-resistant infections.
Area of Science:
- Microbiology
- Biochemistry
- Infectious Diseases
Background:
- Pseudomonas aeruginosa (P. aeruginosa) is a common cause of difficult-to-treat nosocomial infections due to biofilm formation and antibiotic resistance.
- Antimicrobial peptides (AMPs) are emerging as promising therapeutic agents.
- Gp28, a phage-derived AMP, shows activity similar to human LL-37, prompting investigation into its efficacy against P. aeruginosa.
Purpose of the Study:
- To evaluate the antibacterial activity of gp28 against P. aeruginosa.
- To assess gp28's ability to disrupt P. aeruginosa biofilms.
- To determine if gp28 enhances the effectiveness of tobramycin against P. aeruginosa.
Main Methods:
- Bacterial growth inhibition assays determined the minimum inhibitory concentration (MIC) of gp28.
- Crystal violet staining and scanning electron microscopy assessed biofilm disruption.
- Modified time-kill assays evaluated the combined effect of gp28 and tobramycin.
Main Results:
- Gp28 demonstrated significant inhibition of P. aeruginosa planktonic growth with an MIC of 109 μg mL⁻¹.
- Gp28 effectively disrupted established P. aeruginosa biofilms.
- Gp28 treatment increased P. aeruginosa susceptibility to tobramycin.
Conclusions:
- Gp28 exhibits potential as a therapeutic agent against P. aeruginosa.
- Gp28 can be used alone or in combination with tobramycin for treating P. aeruginosa infections.
- Further development of gp28 could offer a new strategy against clinically resistant P. aeruginosa strains.
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