LuxS-mediated quorum sensing in Borrelia burgdorferi, the lyme disease spirochete.
The establishment of Borrelia burgdorferi infection involves numerous interactions between the bacteria and a variety of vertebrate host and arthropod vector tissues. This complex process requires regulated synthesis of many bacterial proteins. We now demonstrate that these spirochetes utilize a LuxS/autoinducer-2 (AI-2)-based quorum-sensing mechanism to regulate protein expression, the first system of cell-cell communication to be described in a spirochete. The luxS gene of B. burgdorferi was identified and demonstrated to encode a functional enzyme by complementation of an Escherichia coli luxS mutant. Cultured B. burgdorferi responded to AI-2 by altering the expression levels of a large number of proteins, including the complement regulator factor H-binding Erp proteins. Through this mechanism, a population of Lyme disease spirochetes may synchronize production of specific proteins needed for infection processes.
Department of Microbiology, Immunology, and Molecular Genetics, University of Kentucky College of Medicine, Lexington 40536-0298, USA. bstev0@uky.edu
Brian
B
Stevenson
Kelly
K
Babb
D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D025065:Borrelia burgdorferi / Q000235:genetics / Q000378:metabolism*; D013437:Carbon-Sulfur Lyases; D006714:Homoserine / Q000031:analogs & derivatives* / Q000378:metabolism*; D007783:Lactones / Q000378:metabolism*; D008193:Lyme Disease / Q000382:microbiology; D008969:Molecular Sequence Data
D001426:Bacterial Proteins; D007783:Lactones; C091088:N-octanoylhomoserine lactone; D006714:Homoserine; D013437:Carbon-Sulfur Lyases; C117753:LuxS protein, Bacteria