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A new Pseudomonas quinolone signal (PQS) binding partner: MexG

James T Hodgkinson1, Jeremy Gross2, Ysobel R Baker1

  • 1Department of Chemistry , University of Cambridge , Lensfield Road , Cambridge , CB2 1EW , UK.

Chemical Science
|June 30, 2017
PubMed

Insights

Researchers developed new tools to study quorum sensing in Pseudomonas aeruginosa. These tools identified a new interaction between the Pseudomonas quinolone signal (PQS) and the MexG protein, suggesting PQS has multiple cellular targets.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Chemical Biology

Background:

  • Pseudomonas aeruginosa is an opportunistic pathogen that uses quorum sensing for virulence regulation.
  • Key quorum sensing molecules are the Pseudomonas quinolone signal (PQS) and its precursor HHQ.
  • PqsR is the only known receptor for PQS and HHQ.

Purpose of the Study:

  • To synthesize PQS and HHQ affinity probes for chemical proteomic analysis.
  • To identify novel binding partners of PQS and HHQ.
  • To investigate the interaction between PQS and the MexG protein.

Main Methods:

  • Synthesis of PQS and HHQ affinity probes.
  • In vitro capture of PqsR using the PQS affinity probe.
  • Purification and in vitro characterization of MexG's binding to PQS and HHQ.

Main Results:

  • The PQS affinity probe successfully captured PqsR in vitro.
  • A novel interaction between PQS and the RND efflux pump protein MexG was identified.
  • MexG was confirmed to bind PQS and HHQ in vitro.

Conclusions:

  • PQS may interact with multiple protein targets within Pseudomonas aeruginosa.
  • The developed affinity probes provide valuable tools for studying quinolone signaling.
  • These findings advance our understanding of quorum sensing regulation in P. aeruginosa.

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