David A. Rasko,Cristiano G. Moreira,De Run Li,Nicola C. Reading,Jennifer M. Ritchie,Matthew K. Waldor,Noelle S. Williams,Ron Taussig,Shuguang Wei,Michael G. Roth,David T. Hughes,Jason F. Huntley,Maggy Fina,John R. Falck,Vanessa Sperandio
出处
期刊:Science [American Association for the Advancement of Science (AAAS)] 日期:2008-08-21卷期号:321 (5892): 1078-1080被引量:485
Many bacterial pathogens rely on a conserved membrane histidine sensor kinase, QseC, to respond to host adrenergic signaling molecules and bacterial signals in order to promote the expression of virulence factors. Using a high-throughput screen, we identified a small molecule, LED209, that inhibits the binding of signals to QseC, preventing its autophosphorylation and consequently inhibiting QseC-mediated activation of virulence gene expression. LED209 is not toxic and does not inhibit pathogen growth; however, this compound markedly inhibits the virulence of several pathogens in vitro and in vivo in animals. Inhibition of signaling offers a strategy for the development of broad-spectrum antimicrobial drugs.