Journal
MOLECULAR MICROBIOLOGY
Volume 114, Issue 3, Pages 423-442Publisher
WILEY
DOI: 10.1111/mmi.14519
Keywords
ClpXP; microbial interspecies interactions; proteolysis; Pseudomonas aeruginosa; quorum sensing
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Funding
- National Natural Science Foundation of China [31670136, 31870127, 81861138047, 81661138004]
- Ministry of Science and Technology of the People's Republic of China [2016YFA0501503]
- State Key Laboratory of Drug Research [SIMM2003ZZ-03]
- Science and Technology Commission of Shanghai Municipality [19JC1416400]
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Intracellular protein degradation is essential for the survival of all organisms, but its role in interspecies interaction is unknown. Here, we show that the ClpXP protease of Pseudomonas aeruginosa suppresses its antimicrobial activity against Staphylococcus aureus, a common pathogen co-isolated with P. aeruginosa from polymicrobial human infections. Using proteomic, biochemical, and molecular genetic approaches, we found that this effect is due to the inhibitory effects of ClpXP on the quorum sensing (QS) of P. aeruginosa, mainly by degrading proteins (e.g., PhnA, PhnB, PqsR, and RhlI) which are critical for the production of QS signal molecules PQS and C4-HSL. We provide evidence that co-culturing with S. aureus induces a decrease in the activity of ClpXP in P. aeruginosa, an effect which was also achieved by the treatment of P. aeruginosa with N-acetylglucosamine (GlcNAc), a widespread chemical present on the surface of diverse cell types from bacteria to humans. These findings extend the range of biological events governed by proteolytic machinery to microbial community structure, thus also suggesting that a chemical-induced alteration of protein homeostasis is a mechanism for interspecies interactions.
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