Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase

Dong, Y.H. and Wang, L.H. and Xu, J.L. and et al, . (2001) Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase. Nature, 411 (6839). pp. 813-817.

[img] PDF - Published Version
Restricted to ICRISAT researchers only

Abstract

Bacterial cells sense their population density through a sophisticated cell–cell communication system and trigger expression of particular genes when the density reaches a threshold. This type of gene regulation, which controls diverse biological functions including virulence, is known as quorum sensing1, 2. Quorum-sensing signals, such as acyl-homoserine lactones (AHLs), are the essential components of the communication system. AHLs regulate virulence gene expression in a range of plant and animal (including human) bacterial pathogens3, 4, 5, 6, 7, 8, 9. AHL-producing tobacco restored the pathogenicity of an AHL-negative mutant of Erwinia carotovora10. Different bacterial species may produce different AHLs, which vary in the length and substitution of the acyl chain but contain the same homoserine lactone moiety. Here we show that the acyl-homoserine lactonase (AHL-lactonase), a new enzyme from Bacillus sp.11, inactivates AHL activity by hydrolysing the lactone bond of AHLs. Plants expressing AHL-lactonase quenched pathogen quorum-sensing signalling and showed significantly enhanced resistance to E. carotovora infection. Our results highlight a promising potential to use quorum-sensing signals as molecular targets for disease control, thereby broadening current approaches for prevention of bacterial infections

Item Type: Article
Author Affiliation: Laboratory of Biosignals and Bioengineering, Institute of Molecular Agrobiology, National University of Singapore, 1 Research Link, 117604, Singapore
Subjects: Plant Protection
Divisions: Other Crops
Depositing User: Ms K Syamalamba
Date Deposited: 02 Jul 2014 10:48
Last Modified: 02 Jul 2014 10:48
Official URL: http://dx.doi.org/10.1038/35081101
URI: http://eprints.icrisat.ac.in/id/eprint/13303

Actions (login required)

View Item View Item