Identification of new quorum sensing autoinducer binding partners in Pseudomonas aeruginosa using photoaffinity probes

Baker, Ysobel R; Hodgkinson, James T.; Florea, Bogdan I.; Alza, Esther; Galloway, Wrjd; Grimm, Larson; Geddis, SM; Overkleeft, HS; Welch, Martin; Spring, David R.

doi:10.1039/c7sc01270e

Cited by 24 publications

(14 citation statements)

References 68 publications

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“…In addition, PQS not only affects cells by altering the transcriptional profiles of genes, but also binds directly to hundreds of previously unrecognized protein partners in the cell. These observations are the first to demonstrate that PQS may directly interact with several key virulence pathways (Hodgkinson et al, 2016 ; Baker et al, 2017 ; Dandela et al, 2018 ). Despite the great efforts made in PQS research, both in vitro and in vivo , its precise role remains poorly understood.…”

Section: Introductionmentioning

confidence: 84%

The Pseudomonas Quinolone Signal (PQS): Not Just for Quorum Sensing Anymore

Lin

Cheng

Wang

et al. 2018

Front. Cell. Infect. Microbiol.

208

193

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Section: Introductionmentioning

confidence: 84%

The Pseudomonas Quinolone Signal (PQS): Not Just for Quorum Sensing Anymore

Lin

Cheng

Wang

et al. 2018

Front. Cell. Infect. Microbiol.

208

193

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“…The QS phenomenon operates via the synthesis of small molecular weight molecules, which then bind to their partner proteins to enable the protein to exhibit its function. P. aeruginosa produces the QS molecule N ‐butyryl‐ L ‐homoserine lactone (BHL) which is also referred to as the autoinducer ligand . In previous studies, it was mentioned that RhlR had dimerisation ability in the presence of the autoinducer ligand .…”

Section: Introductionmentioning

confidence: 99%

Identification of ligand binding activity and DNA recognition by RhlR protein from opportunistic pathogen Pseudomonas aeruginosa—a molecular dynamic simulation approach

Chowdhury

Bagchi

2018

J of Molecular Recognition

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RhlR protein from opportunistic pathogen Pseudomonas aeruginosa is involved in the transcription of virulence genes of the organism. The RhlR protein functions as a dimer and binds to the cognate promoter DNA with the help of an autoinducer ligand BHL to initiate the transcription of the virulence genes. Till date, there are no reports that detail the mechanism of virulence gene expression by RhlR protein in P. aeruginosa. In this work, we tried to analyse the molecular aspects of the various binding interactions of the RhlR protein while formimg the dimmer as well as with the promoter DNA. We analysed the mode of dimerisation of the RhlR protein and its binding interactions with the autoinducer BHL ligand. From our analyses, we could identify the potential amino acid residues which are involved in the binding interactions. We also predicted how the autoinducer BHL would help in making contacts with the DNA as well as with itself. Thus, the autoinducer BHL would serve as an important mediator of molecular interactions involved in binding the RhlR protein to itself as well as with the promoter DNA. Therefore, any other molecule which would be able to compete with the autoinducer ligand BHL to bind to RhlR protein but would not let the RhlR protein bind the promoter DNA would be an ideal drug candidate to prevent the transcription process of the virulence genes in P. aeruginosa. Our future aim is to predict suitable ligands which would compete with BHL to thwart the transcription process.

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“…In the course of preparation of this manuscript a valuable similar study was published by Spring and coworkers, 27 in which different PQS- and HHQ-based probes (with azide-containing quinolones) were evaluated in P. aeruginosa . Interestingly, we identified all the proteins from the former article, with the exception of the RhrR transcriptional regulator and the protease Pfpl, suggesting that there is a significant overlap in the proteome coverage between the different probes.…”

Section: Resultsmentioning

confidence: 99%