ArticleAntimicrobial agents and chemotherapy2013
A quinazoline-2,4-diamino analog suppresses Vibrio cholerae flagellar motility by interacting with motor protein PomB and induces envelope stress.
Article in Antimicrobial agents and chemotherapy, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Targeting motility and chemotaxis as a strategy to combat bacterial pathogens.Microbial biotechnology · 2023Article
- Motility of Vibrio spp.: regulation and controlling strategies.Applied microbiology and biotechnology · 2020Review
- Synthesis, Characterization, Antibacterial Activity, and Computer-Aided Design of Novel Quinazolin-2,4-dione Derivatives as Potential Inhibitors AgainstEvolutionary bioinformatics online · 2020Article
- Structural changes of bacterial nanocellulose pellicles induced by genetic modification of Komagataeibacter hansenii ATCC 23769.Applied microbiology and biotechnology · 2019Article
- The Bioactive Lipid (S)-Sebastenoic Acid Impacts Motility and Dispersion inCanadian journal of chemistry · 2018Article
- Flagellar motility, extracellular proteases and Vibrio cholerae detachment from abiotic and biotic surfaces.Microbial pathogenesis · 2017Article
- 3-Amino 1,8-naphthalimide, a structural analog of the anti-cholera drug virstatin inhibits chemically-biased swimming and swarming motility in vibrios.Microbes and infection · 2017Article
- Vibrio cholerae Biofilms and Cholera Pathogenesis.PLoS neglected tropical diseases · 2016Review
- Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Vibrio cholerae strains of serogroups O1 and O139, the causative agents of the diarrheal illness cholera, express a single polar flagellum powered by sodium motive force and require motility to colonize and spread along the small intestine. In a previous study, we described a high-throughput assay for screening for small molecules that selectively inhibit bacterial motility and identified a family of quinazoline-2,4-diamino analogs (Q24DAs) that (i) paralyzed the sodium-driven polar flagellum of Vibrios and (ii) diminished cholera toxin secreted by El Tor biotype V. cholerae. In this study, we provide evidence that a Q24DA paralyzes the polar flagellum by interacting with the motor protein PomB. Inhibition of motility with the Q24DA enhanced the transcription of the cholera toxin genes in both biotypes. We also show that the Q24DA interacts with outer membrane protein OmpU and other porins to induce envelope stress and expression of the extracellular RNA polymerase sigma factor σ(E). We suggest that Q24DA-induced envelope stress could affect the correct folding, assembly, and secretion of pentameric cholera toxin in El Tor biotype V. cholerae independently of its effect on motility.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.