| Home > Publications database > Secreted retropepsin-like enzymes are essential for stress tolerance and biofilm formation in Pseudomonas aeruginosa |
| Typ | Amount | VAT | Currency | Share | Status | Cost centre |
| APC | 3340.00 | 0.00 | USD | 100.00 % | (Zahlung erfolgt) | 810 / 476151 |
| Sum | 3340.00 | 0.00 | (see parts above) | |||
| Total | 3340.00 |
| Journal Article | PUBDB-2024-05704 |
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2025
American Society for Microbiology
Washington, DC
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Please use a persistent id in citations: doi:10.1128/mbio.00872-25 doi:10.3204/PUBDB-2024-05704
Abstract: Proteases regulate important biological functions. Here we present the structural andfunctional characterization of three novel aspartic proteases in Pseudomonas aeruginosa. Weshow that these proteases have structural hallmarks of retropepsin peptidases and playredundant roles for cell survival under hypoosmotic stress conditions. Consequently, we namedthem retropepsin-like osmotic stress tolerance peptidases (Rlo). Our research shows that whileRlo proteases are homologous to RimB, an aspartic peptidase involved in rhizospherecolonization and plant infection, they contain N-terminal signal peptides and perform separatebiological functions. Mutants lacking all three secreted Rlo peptidases show defects in antibioticresistance, biofilm formation, and cell morphology. These defects are rescued by mutations in theinactive transglutaminase transmembrane protein RloB and the cytoplasmic ATP-grasp proteinRloC, two previously uncharacterized genes in the same operon as one of the Rlo proteases.These studies identify Rlo proteases and rlo operon products as critical factors in clinicallyrelevant processes, making them appealing drug targets to combat Pseudomonas infections.
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