ArticleJournal of bacteriology2013
The Francisella tularensis FabI enoyl-acyl carrier protein reductase gene is essential to bacterial viability and is expressed during infection.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- TPR1, a novel rifampicin derivative, demonstrates efficacy alone and in combination with doxycycline against the NIAID Category A priority pathogenJAC-antimicrobial resistance · 2021Article
- Structural approaches to pathway-specific antimicrobial agents.Translational research : the journal of laboratory and clinical medicine · 2020Review
- Exploring the Diversity Within the GenusFrontiers in microbiology · 2020Article
- Small-Molecule Inhibition of theACS chemical biology · 2019Article
- The Fatty Acid Synthesis Protein Enoyl-ACP Reductase II (FabK) is a Target for Narrow-Spectrum Antibacterials for Clostridium difficile Infection.ACS infectious diseases · 2019Article
- Determination of absolute configuration and binding efficacy of benzimidazole-based FabI inhibitors through the support of electronic circular dichroism and MM-GBSA techniques.Bioorganic & medicinal chemistry letters · 2018Article
- Structural characterization of Porphyromonas gingivalis enoyl-ACP reductase II (FabK).Acta crystallographica. Section F, Structural biology communications · 2018Article
- A novel series of enoyl reductase inhibitors targeting the ESKAPE pathogens, Staphylococcus aureus and Acinetobacter baumannii.Bioorganic & medicinal chemistry · 2018Article
- Benzimidazole-Based FabI Inhibitors: A Promising Novel Scaffold for Anti-staphylococcal Drug Development.ACS infectious diseases · 2017Article
- The unusual substrate specificity of a virulence associated serine hydrolase from the highly toxic bacterium,Biochemistry and biophysics reports · 2016Article
- Structural and biological evaluation of a novel series of benzimidazole inhibitors of Francisella tularensis enoyl-ACP reductase (FabI).Bioorganic & medicinal chemistry letters · 2015Article
- Bis-indolic compounds as potential new therapeutic alternatives for tularaemia.Frontiers in cellular and infection microbiology · 2014Article
- Inefficient translation renders the Enterococcus faecalis fabK enoyl-acyl carrier protein reductase phenotypically cryptic.Journal of bacteriology · 2014Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Francisella tularensis is classified as a category A priority pathogen and causes fatal disseminated disease in humans upon inhalation of less than 50 bacteria. Although drugs are available for treatment, they are not ideal because of toxicity and route of delivery, and in some cases patients relapse upon withdrawal. We have an ongoing program to develop novel FAS-II FabI enoyl-ACP reductase enzyme inhibitors for Francisella and other select agents. To establish F. tularensis FabI (FtFabI) as a clinically relevant drug target, we demonstrated that fatty acid biosynthesis and FabI activity are essential for growth even in the presence of exogenous long-chain lipids and that FtfabI is not transcriptionally altered in the presence of exogenous long-chain lipids. Inhibition of FtFabI or fatty acid synthesis results in loss of viability that is not rescued by exogenous long-chain lipid supplementation. Importantly, whole-genome transcriptional profiling of F. tularensis with DNA microarrays from infected tissues revealed that FtfabI and de novo fatty acid biosynthetic genes are transcriptionally active during infection. This is the first demonstration that the FabI enoyl-ACP-reductase enzyme encoded by F. tularensis is essential and not bypassed by exogenous fatty acids and that de novo fatty acid biosynthetic components encoded in F. tularensis are transcriptionally active during infection in the mouse model of tularemia.
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