ArticleBioorganic & medicinal chemistry2013
Chrysophaentins are competitive inhibitors of FtsZ and inhibit Z-ring formation in live bacteria.
Article in Bioorganic & medicinal chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 53 citations in OpenAlex.
- FtsZ as a novel target for antibiotics development: Promises and challenges.Acta pharmaceutica Sinica. B · 2025Review
- The genome of antibiotic-producing colonies of the Pelagophyte alga Chrysophaeum taylorii reveals a diverse and non-canonical capacity for secondary metabolism.Scientific reports · 2023Article
- Filamentous temperature sensitive mutant Z: a putative target to combat antibacterial resistance.RSC advances · 2023Review
- Models versus pathogens: how conserved is the FtsZ in bacteria?Bioscience reports · 2023Review
- Properties of Configurationally Stable Atropoenantiomers in Macrocyclic Natural Products and the Chrysophaentin Family.Accounts of chemical research · 2023Review
- β-Lactams from the Ocean.Marine drugs · 2023Review
- Naturally Occurring Organohalogen Compounds-A Comprehensive Review.Progress in the chemistry of organic natural products · 2023Review
- The Search for Antibacterial Inhibitors Targeting Cell Division Protein FtsZ at Its Nucleotide and Allosteric Binding Sites.Biomedicines · 2022Review
- Filamentous Thermosensitive Mutant Z: An Appealing Target for Emerging Pathogens and a Trek on Its Natural Inhibitors.Biology · 2022Review
- Targeting the Achilles Heel of FtsZ: The Interdomain Cleft.Frontiers in microbiology · 2021Review
- Synthesis of 9-Dechlorochrysophaentin A Enables Studies Revealing Bacterial Cell Wall Biosynthesis Inhibition Phenotype inJournal of the American Chemical Society · 2020Article
- Molecule Property Analyses of Active Compounds forJournal of medicinal chemistry · 2020Review
- A key bacterial cytoskeletal cell division protein FtsZ as a novel therapeutic antibacterial drug target.Bosnian journal of basic medical sciences · 2020Review
- Targeting Bacterial Cell Division: A Binding Site-Centered Approach to the Most Promising Inhibitors of the Essential Protein FtsZ.Antibiotics (Basel, Switzerland) · 2020Review
- Recent Progress in the Development of Small-Molecule FtsZ Inhibitors as Chemical Tools for the Development of Novel Antibiotics.Antibiotics (Basel, Switzerland) · 2019Review
- Antimicrobial Chrysophaentin Analogs Identified from Laboratory Cultures of the Marine Microalga Chrysophaeum taylorii.Journal of natural products · 2019Article
- Indole-core-based novel antibacterial agent targeting FtsZ.Infection and drug resistance · 2019Article
- Competitive Fitness of Essential Gene Knockdowns Reveals a Broad-Spectrum Antibacterial Inhibitor of the Cell Division Protein FtsZ.Antimicrobial agents and chemotherapy · 2018Article
- Study of Benzofuroquinolinium Derivatives as a New Class of Potent Antibacterial Agent and the Mode of Inhibition Targeting FtsZ.Frontiers in microbiology · 2018Article
- Review
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
The bacterial cell division protein FtsZ polymerizes in a GTP-dependent manner to form a Z-ring that marks the plane of division. As a validated antimicrobial target, considerable efforts have been devoted to identify small molecule FtsZ inhibitors. We recently discovered the chrysophaentins, a novel suite of marine natural products that inhibit FtsZ activity in vitro. These natural products along with a synthetic hemi-chrysophaentin exhibit strong antimicrobial activity toward a broad spectrum of Gram-positive pathogens. To define their mechanisms of FtsZ inhibition and determine their in vivo effects in live bacteria, we used GTPase assays and fluorescence anisotropy to show that hemi-chrysophaentin competitively inhibits FtsZ activity. Furthermore, we developed a model system using a permeable Escherichia coli strain, envA1, together with an inducible FtsZ-yellow fluorescent protein construct to show by fluorescence microscopy that both chrysophaentin A and hemi-chrysophaentin disrupt Z-rings in live bacteria. We tested the E. coli system further by reproducing phenotypes observed for zantrins Z1 and Z3, and demonstrate that the alkaloid berberine, a reported FtsZ inhibitor, exhibits auto-fluorescence, making it incompatible with systems that employ GFP or YFP tagged FtsZ. These studies describe unique examples of nonnucleotide, competitive FtsZ inhibitors that disrupt FtsZ in vivo, together with a model system that should be useful for in vivo testing of FtsZ inhibitor leads that have been identified through in vitro screens but are unable to penetrate the Gram-negative outer membrane.
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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.