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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Hwang, Ingyu Rhee, Sangkee Lee, Jeehyun Kim, Hongsup Igarashi, Jun Suga, Hiroaki Chung, Jiwoung Yu, Sangheon Moon, Jae Sun Choi, Okhee Kim, Jinwoo Goo, Eunhye |
| Description | Author Affiliation: Chung J ( Department of Agricultural Biotechnology, Seoul National University, Seoul 151-921, Korea.); |
| Abstract | Quorum sensing (QS) controls certain behaviors of bacteria in response to population density. In gram-negative bacteria, QS is often mediated by N-acyl-L-homoserine lactones (acyl-HSLs). Because QS influences the virulence of many pathogenic bacteria, synthetic inhibitors of acyl-HSL synthases might be useful therapeutically for controlling pathogens. However, rational design of a potent QS antagonist has been thwarted by the lack of information concerning the binding interactions between acyl-HSL synthases and their ligands. In the gram-negative bacterium Burkholderia glumae, QS controls virulence, motility, and protein secretion and is mediated by the binding of N-octanoyl-L-HSL (C8-HSL) to its cognate receptor, TofR. C8-HSL is synthesized by the acyl-HSL synthase TofI. In this study, we characterized two previously unknown QS inhibitors identified in a focused library of acyl-HSL analogs. Our functional and X-ray crystal structure analyses show that the first inhibitor, J8-C8, binds to TofI, occupying the binding site for the acyl chain of the TofI cognate substrate, acylated acyl-carrier protein. Moreover, the reaction byproduct, 5'-methylthioadenosine, independently binds to the binding site for a second substrate, S-adenosyl-L-methionine. Closer inspection of the mode of J8-C8 binding to TofI provides a likely molecular basis for the various substrate specificities of acyl-HSL synthases. The second inhibitor, E9C-3oxoC6, competitively inhibits C8-HSL binding to TofR. Our analysis of the binding of an inhibitor and a reaction byproduct to an acyl-HSL synthase may facilitate the design of a new class of QS-inhibiting therapeutic agents. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 29 |
| Volume Number | 108 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2011-07-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | 4-Butyrolactone Analogs & Derivatives Bacterial Proteins Antagonists & Inhibitors Burkholderia Metabolism Protein Binding Quorum Sensing Physiology S-Adenosylmethionine Transcription Factors Crystallography, X-Ray Fluorescence Homoserine Lactones Substrate Specificity Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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