Pseudomonas quinolone signal receptor (PqsR) (PqsR)

Pseudomonas quinolone signal receptor (PqsR), also known as Multiple virulence factor regulator (MvfR), is a LysR-type transcriptional regulator (LTTR) that plays a pivotal role in the quorum sensing (QS) network of the opportunistic pathogen Pseudomonas aeruginosa (UniProt P0C1P1). It is activated by the signaling molecules 2-heptyl-4-hydroxyquinoline (HHQ) and the Pseudomonas quinolone signal (PQS), which bind to its C-terminal ligand-binding domain (PubMed: 23835341). Once activated, PqsR binds to the promoter of the pqsABCDE operon, driving the synthesis of alkylquinolones and regulating the expression of numerous virulence factors such as pyocyanin, lectins, and elastase, which are critical for host tissue damage and immune evasion (PubMed: 15995187). PqsR is also a key regulator of biofilm maturation and antibiotic tolerance, making it a significant factor in chronic infections like those found in cystic fibrosis and non-healing wounds (PubMed: 25155930). Because PqsR controls virulence rather than essential metabolic processes, it is considered a high-priority target for anti-virulence therapy, aiming to reduce pathogenicity while minimizing the selective pressure that leads to traditional antibiotic resistance (PubMed: 30104683). Several classes of small-molecule inhibitors, including quinazolinone and benzamide-benzimidazole derivatives, have been developed to antagonize PqsR, showing promise in reducing bacterial burden and increasing the efficacy of co-administered antibiotics in vivo (PubMed: 24931440).

Other names

Multiple virulence factor regulatorMvfRLysR-type transcriptional regulator PqsRTranscription factor PqsR

Antagonism of the PqsR ligand-binding domain to prevent activation by HHQ/PQS, thereby inhibiting the expression of the pqsABCDE operon and downstream virulence factors (PubMed: 24931440).