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An Inhibitor of Gram-Negative Bacterial Virulence Protein Secretion
Open accessAbstract
SUMMARY Bacterial virulence mechanisms are attractive targets for antibiotic development, because they are required for the pathogenesis of numerous global infectious disease agents. The bacterial secretion systems used to assemble the surface structures that promote adherence and deliver protein virulence effectors to host cells could comprise one such therapeutic target. In this study, we developed and performed a high-throughput screen (HTS) of small molecule libraries and identified a small molecule, a 2-imino-5-arylidene thiazolidinone that blocked secretion and virulence functions of a wide array of animal and plant Gram-negative bacterial pathogens. This compound inhibited type III secretion-dependent functions, with the exception of flagellar motility, and Type II secretion-dependent functions, suggesting that the target of the compound could be an outer membrane component conserved between these two secretion systems. This work provides a proof of concept that compounds with a broad spectrum of activity against Gram-negative bacterial secretion systems could be developed to prevent and treat bacterial diseases.
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Citations
Cites
Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1β via Ipaf
Miao, E. A., Alpuche-Aranda, C. M., Dors, M., Clark, A. E., Bader, M. W., Miller, S. I., & Aderem, A. (2006) · Nature Immunology · doi:10.1038/ni1344 · Cited by 1,127 · cited 1×
“The enteric pathogens Salmonella and Shigella stimulate caspase-1-mediated cell death as a result of T3S-mediated translocation (Miao et al., 2006).”
Self-citation
Cited by
Anti-virulence strategies to combat bacteria-mediated disease
Rasko, D. A., & Sperandio, V. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd3013 · Cited by 1,373
Langdon, A., Crook, N., & Dantas, G. (2016) · Genome Medicine · doi:10.1186/s13073-016-0294-z · Cited by 912
Alkaloids: An overview of their antibacterial, antibiotic-enhancing and antivirulence activities
Cushnie, T. P. T., Cushnie, B., & Lamb, A. J. (2014) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2014.06.001 · Cited by 894
Targeting virulence: can we make evolution-proof drugs?
Allen, R. C., Popat, R., Diggle, S. P., & Brown, S. P. (2014) · Nature Reviews Microbiology · doi:10.1038/nrmicro3232 · Cited by 532
Metadata
- Authors
- Felise, H. B., Nguyen, H. V., Pfuetzner, R. A., Barry, K. C., Jackson, S. R., Blanc, M.-P., Bronstein, P. A., Kline, T., & Miller, S. I.
- Venue
- Cell Host & Microbe
- Publisher
- Elsevier BV
- Published
- 2008-10
- Volume
- 4
- Issue
- 4
- Pages
- 325-336
- ISSN
- 1931-3128 (ISSN-L)
- OpenAlex
- W2024180691
- Cited by
- 163
- References
- 1
- FWCI
- 5.88
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Felise, H. B., Nguyen, H. V., Pfuetzner, R. A., Barry, K. C., Jackson, S. R., Blanc, M.-P., Bronstein, P. A., Kline, T., & Miller, S. I. (2008). An Inhibitor of Gram-Negative Bacterial Virulence Protein Secretion. Cell Host & Microbe. https://doi.org/10.1016/j.chom.2008.08.001
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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