The two first authors have equally contributed to this work and are listed by alphabetic order.
N-hexanoyl-l-homoserine lactone, a mediator of bacterial quorum-sensing regulation, exhibits plant-dependent stability and may be inactivated by germinating Lotus corniculatus seedlings
Version of Record online: 5 JAN 2006
FEMS Microbiology Ecology
Volume 52, Issue 1, pages 13–20, March 2005
How to Cite
Delalande, L., Faure, D., Raffoux, A., Uroz, S., D'Angelo-Picard, C., Elasri, M., Carlier, A., Berruyer, R., Petit, A., Williams, P. and Dessaux, Y. (2005), N-hexanoyl-l-homoserine lactone, a mediator of bacterial quorum-sensing regulation, exhibits plant-dependent stability and may be inactivated by germinating Lotus corniculatus seedlings. FEMS Microbiology Ecology, 52: 13–20. doi: 10.1016/j.femsec.2004.10.005
- Issue online: 5 JAN 2006
- Version of Record online: 5 JAN 2006
- Received 25 May 2004, Revised 30 September 2004, Accepted 6 October 2004
- N-acyl homoserine lactone;
- Quorum sensing;
The half-life of N-hexanoyl-l-homoserine lactone (C6-HSL) was determined under various pH and temperature conditions, and in several plant environments. C6-HSL was sensitive to alkaline pH, a process that was also temperature-dependent. In addition, C6-HSL disappeared from plant environments, i.e. axenic monocot and dicot plants cultivated under gnotobiotic, hydroponic conditions, albeit with variable kinetics. The disappearance was rapid at the root system of legume plants such as clover or Lotus, and slow or non-existent at the root system of monocots such as wheat or corn. These variable kinetics were not dependent upon pH changes that may have affected the growth media of the plants. Furthermore, C6-HSL did not accumulate in the plant, and the plant did not produce inhibitors of the C6-HSL signal. HPLC analyses revealed that C6-HSL disappeared from the media, and hence, Lotus exhibited a natural C6-HSL inactivating ability. This ability was not specific for C6-HSL and allowed the degradation of other N-acyl-homoserine lactones such as 3-oxo-C6-HSL, 3-oxo-octanoyl-HSL and 3-oxo-decanoyl-HSL. Preliminary investigation revealed that the inactivating ability is temperature-dependant and possibly of enzymatic origin.