Welch, Martin3; Hodgkinson, James T.3; Gross, Jeremy3; Spring, David R.3; Sams, Thomas4
1 Department of Electrical Engineering, Technical University of Denmark2 Biomedical Engineering, Department of Electrical Engineering, Technical University of Denmark3 University of Cambridge4 Copenhagen Center for Health Technology, Center, Technical University of Denmark
The Pseudomonas aeruginosa quinolone signal (PQS) is a quorum sensing molecule that plays an important role in regulating the virulence of this organism. We have purified the ligand binding domain of the receptor PqsRLBD for PQS and have used Förster resonance energy transfer fluorimetry and kinetic modeling to characterize the ligand binding in vitro. The dissociation constant for binding of PQS to a ligand binding site in (PqsRLBD)2 dimers was determined to be 1.2 ± 0.3 μM. We found no cooperativity in the consecutive binding of two ligand molecules to the dimer.
Biochemistry, 2013, Vol 52, Issue 25, p. 4433-4438