| Autor: |
Wannasrichan W, Krobthong S, Morgan CJ, Armbruster EG, Gerovac M, Yingchutrakul Y, Wongtrakoongate P, Vogel J, Aonbangkhen C, Nonejuie P, Pogliano J, Chaikeeratisak V |
| Jazyk: |
angličtina |
| Zdroj: |
BioRxiv : the preprint server for biology [bioRxiv] 2024 Jun 16. Date of Electronic Publication: 2024 Jun 16. |
| DOI: |
10.1101/2024.06.15.599175 |
| Abstrakt: |
Antibacterial proteins inhibiting Pseudomonas aeruginosa have been identified in various phages and explored as antibiotic alternatives. Here, we isolated a phiKZ-like phage, Churi, which encodes 364 open reading frames. We examined 15 early-expressed phage proteins for their ability to inhibit bacterial growth, and found that gp335, closely related to phiKZ-gp14, exhibits antibacterial activity. Similar to phiKZ-gp14, recently shown to form a complex with the P. aeruginosa ribosome, we predict experimentally that gp335 interacts with ribosomal proteins, suggesting its involvement in protein translation. GFP-tagged gp335 clusters around the phage nucleus as early as 15 minutes post-infection and remains associated with it throughout the infection, suggesting its role in protein expression in the cell cytoplasm. CRISPR-Cas13-mediated deletion of gp355 reveals that the mutant phage has a prolonged latent period. Altogether, we demonstrate that gp335 is an antibacterial protein of nucleus-forming phages that associates with the ribosomes at the phage nucleus. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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