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Authors

Layla Abbud

Abstract

Endolysins are proteins that degrade bacterial cell walls. They are encoded on the genome of bacteriophages (viruses that infect and kill bacteria). At the end of the lytic cycle of a bacteriophage, endolysins cut the peptidoglycan layer of the bacterial cell wall, allowing the release of viral progeny. Pseudomonas aeruginosa is a well-known multidrug-resistant human pathogen that causes serious problems, especially in patients diagnosed with cystic fibrosis (CF). One property of P. aeruginosa is the production of biofilms, which is a defense against antibiotics. Previous research has shown that endolysins from bacteriophages can degrade biofilms. The endolysin protein from Persinger, a phage that infects P. aeruginosa, was purified, and biofilm eradication assays of the endolysin were carried out. The endolysin protein showed biofilm disruption activity against P. aeruginosa clinical samples UVA1, UVA4, and biofilm super-former PAO1ΔwspF-GFP. Protein structure prediction and characterization of the Persinger endolysin along with another LysPA26 endolysin known to have biofilm eradication activity were analyzed using AlphaFold and PyMol. An additional 4 endolysin proteins were characterized using ClustalOmega, PSIPRED, and Protpi software. The Persinger endolysin is predicted to have 8 alpha helix domains separated by loops and turns. LysPA26 is predicted to have 7 alpha helix domains and 4 beta sheets separated by loops and turns. Together, these findings demonstrate that the novel Persinger endolysin exhibits significant biofilm eradication activity against multi-drug resistant P. aeruginosa and possesses distinct structural features that support its potential development as a targeted antimicrobial therapy.

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