TY - JOUR
T1 - Salmonella typhimurium recognizes a chemically distinct form of the bacterial quorum-sensing signal AI-2
AU - Miller, Stephen T.
AU - Xavier, Karina B.
AU - Campagna, Shawn R.
AU - Taga, Michiko E.
AU - Semmelhack, Martin F.
AU - Bassler, Bonnie L.
AU - Hughson, Frederick M.
N1 - Funding Information:
We thank Matt Neiditch, together with Michael Becker and the staff of the National Synchrotron Light Source X25 beamline, for assistance with X-ray data collection; Istvan Pelczer and Maria Borcsik for technical assistance; Melissa Miller for V. harveyi strain MM32; Michael Meijler and Kim Janda (Scripps Research Institute, La Jolla) for advice and communicating results prior to publication; Yigong Shi for helpful comments on the manuscript; and members of our laboratories for advice and discussion. This work was supported by NIH grant AI054442.
PY - 2004/9/10
Y1 - 2004/9/10
N2 - Bacterial populations use cell-cell communication to coordinate community-wide regulation of processes such as biofilm formation, virulence, and bioluminescence. This phenomenon, termed quorum sensing, is mediated by small molecule signals known as autoinducers. While most autoinducers are species specific, autoinducer-2 (AI-2), first identified in the marine bacterium Vibrio harveyi, is produced and detected by many Gram-negative and Gram-positive bacteria. The crystal structure of the V. harveyi AI-2 signaling molecule bound to its receptor protein revealed an unusual furanosyl borate diester. Here, we present the crystal structure of a second AI-2 signal binding protein, LsrB from Salmonella typhimurium. We find that LsrB binds a chemically distinct form of the AI-2 signal, (2R,4S)-2-methyl-2,3,3,4-tetrahydroxytetrahydrofuran (R-THMF), that lacks boron. Our results demonstrate that two different species of bacteria recognize two different forms of the autoinducer signal, both derived from 4,5-dihydroxy-2,3-pentanedione (DPD), and reveal new sophistication in the chemical lexicon used by bacteria in interspecies signaling.
AB - Bacterial populations use cell-cell communication to coordinate community-wide regulation of processes such as biofilm formation, virulence, and bioluminescence. This phenomenon, termed quorum sensing, is mediated by small molecule signals known as autoinducers. While most autoinducers are species specific, autoinducer-2 (AI-2), first identified in the marine bacterium Vibrio harveyi, is produced and detected by many Gram-negative and Gram-positive bacteria. The crystal structure of the V. harveyi AI-2 signaling molecule bound to its receptor protein revealed an unusual furanosyl borate diester. Here, we present the crystal structure of a second AI-2 signal binding protein, LsrB from Salmonella typhimurium. We find that LsrB binds a chemically distinct form of the AI-2 signal, (2R,4S)-2-methyl-2,3,3,4-tetrahydroxytetrahydrofuran (R-THMF), that lacks boron. Our results demonstrate that two different species of bacteria recognize two different forms of the autoinducer signal, both derived from 4,5-dihydroxy-2,3-pentanedione (DPD), and reveal new sophistication in the chemical lexicon used by bacteria in interspecies signaling.
UR - http://www.scopus.com/inward/record.url?scp=4444332516&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=4444332516&partnerID=8YFLogxK
U2 - 10.1016/j.molcel.2004.07.020
DO - 10.1016/j.molcel.2004.07.020
M3 - Article
C2 - 15350213
AN - SCOPUS:4444332516
SN - 1097-2765
VL - 15
SP - 677
EP - 687
JO - Molecular Cell
JF - Molecular Cell
IS - 5
ER -