4.7 Article

Citrinin Is a Potential Quorum Sensing Inhibitor against Pseudomonas aeruginosa

Journal

MARINE DRUGS
Volume 21, Issue 5, Pages -

Publisher

MDPI
DOI: 10.3390/md21050296

Keywords

Pseudomonas aeruginosa; quorum sensing inhibitors; marine fungi; Penicillium sp; JH1; citrinin

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Pseudomonas aeruginosa is an opportunistic pathogen that uses a quorum sensing system to protect itself from antibiotics and environmental stress. A marine fungus, Penicillium sp. JH1, was found to produce a novel quorum sensing inhibitor called citrinin, which can inhibit the production of violacein in Chromobacterium violaceum and three virulence factors in P. aeruginosa. Citrinin can also inhibit biofilm formation and motility of P. aeruginosa, and downregulate the expression of genes associated with quorum sensing.
Pseudomonas aeruginosa is an opportunistic pathogen that infects patients by regulating virulence factors and biofilms through a quorum sensing (QS) system to protect itself from antibiotics and environmental stress. Therefore, the development of quorum sensing inhibitors (QSIs) is expected to become a new strategy for studying drug resistance to P. aeruginosa infections. Marine fungi are valuable resources for screening QSIs. A marine fungus, Penicillium sp. JH1, with anti-QS activity was isolated from the offshore waters of Qingdao (China), and citrinin, a novel QSI, was purified from secondary metabolites of this fungus. Citrinin could significantly inhibit the production of violacein in Chromobacterium violaceum CV12472 and the production of three virulence factors (elastase, rhamnolipid and pyocyanin) in P. aeruginosa PAO1. It could also inhibit the biofilm formation and motility of PAO1. In addition, citrinin downregulated the transcript levels of nine genes (lasI, rhlI, pqsA, lasR, rhlR, pqsR, lasB, rhlA and phzH) associated with QS. Molecular docking results showed that citrinin bound to PqsR and LasR with better affinity than the natural ligands. This study laid a foundation for the further study of the structure optimization and structure-activity relationship of citrinin.

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