Quorum sensing in Vibrio harveyi: probing the specificity of the LuxP binding site.
Quorum sensing activity was investigated in the bacterium Vibrio harveyi using a series of both natural and nonnatural analogs of DPD, the penultimate precursor to autoinducer AI-2. The progression of molecules that were both synthesized and investigated includes enantiomeric variants, carbon-chain extension, and hydroxyl-functional group addition/deletions of DPD. The compilation of these studies reveals a binding cleft that can accommodate a number of different structural variants of DPD, albeit with invariably lower activities.
Lowery
Colin A
CA
Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
McKenzie
Kathleen M
KM
Qi
Longwu
L
Meijler
Michael M
MM
Janda
Kim D
KD
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D002450:Cell Communication / Q000502:physiology*; D006714:Homoserine / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000494:pharmacology; D007783:Lactones / Q000138:chemical synthesis* / Q000494:pharmacology; D013379:Substrate Specificity; D014733:Vibrio / Q000187:drug effects / Q000502:physiology*
D001426:Bacterial Proteins; D007783:Lactones; C090749:LuxP protein, Vibrio; C091088:N-octanoylhomoserine lactone; D006714:Homoserine