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Journal of Bacteriology, July 2008, p. 5137-5141, Vol. 190, No. 14
0021-9193/08/$08.00+0 doi:10.1128/JB.00246-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Department of Microbiology, University of Washington School of Medicine, Seattle, Washington 98195-7242,1 Department of Pharmacology, Program in Biomolecular Structure, University of Colorado Denver, School of Medicine, Aurora, Colorado 80045,2 Bacteriology Division, United States Army Medical Research Institute of Infectious Diseases, Fort Detrick, Maryland 217043
Received 18 February 2008/ Accepted 2 May 2008
Burkholderia mallei has two acyl-homoserine lactone (acyl-HSL) signal generator-receptor pairs and two additional signal receptors, all of which contribute to virulence. We show that B. mallei produces N-3-hydroxy-octanoyl HSL (3OHC8-HSL) but a bmaI3 mutant does not. Recombinant Escherichia coli expressing BmaI3 produces hydroxylated acyl-HSLs, with 3OHC8-HSL being the most abundant compound. In recombinant E. coli, BmaR3 responds to 3OHC8-HSL but not to other acyl-HSLs. These data indicate that the signal for BmaR3-BmaI3 quorum sensing is 3OHC8-HSL.
Published ahead of print on 16 May 2008.
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