The Characterization of a Novel Broad-Spectrum Pseudomonas aeruginosa Receptor Binding Protein Derived from a Chimeric M13 Phage Display Library

As a leading global health concern, antimicrobial resistance threatens the continued reliance on antibiotics to treat bacterial infections in clinical settings. Bacteriophage (or phage) therapy as an alternative antimicrobial strategy has resurfaced in the recent years. Phage therapy relies on the idea that phages are natural viruses against bacteria, having evolved diverse mechanisms to bind, infect, and kill their hosts. Modern approaches to phage therapy use a combination of genetic, chemical, and biomolecular approaches to engineer novel antimicrobial functionalities. In this work, I characterize a novel receptor binding protein, named PAB, that was selected from a phage display library based on its ability to bind a wide variety of clinically isolated, drug- resistant Pseudomonas aeruginosa strains, which are known for their virulence, especially innosocomial infections. It is envisioned that with further characterization and optimization of the PAB protein, chimeric M13 phage displaying PAB on its surface can be applied towards the development of phage-based therapeutics and diagnostic tools against a broad spectrum of P. aeruginosa strains.