ArticleMolecular microbiology2013
Identification and characterization of a periplasmic trilactone esterase, Cee, revealed unique features of ferric enterobactin acquisition in Campylobacter.
Article in Molecular microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 43 citations in OpenAlex.
- Identification and characterization of an invasive, hyper-aerotolerantASM case reports · 2025Article
- Stereospecific control of microbial growth by a combinatoric suite of chiral siderophores.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Contribution of fepABMC microbiology · 2025Article
- Discovery of Peptidic Siderophore Degradation by Screening Natural Product Profiles in Marine-Derived Bacterial Mono- and Cocultures.Biochemistry · 2025Article
- Inactivation of siderophore iron-chelating moieties by the fungal wheat root symbiont Pyrenophora biseptata.Environmental microbiology reports · 2024Article
- Thermostable homologues of the periplasmic siderophore-binding protein CeuE from Geobacillus stearothermophilus and Parageobacillus thermoglucosidasius.Acta crystallographica. Section D, Structural biology · 2023Article
- Assessment of an Enterobactin Conjugate Vaccine in Layers to Protect Their Offspring from Colibacillosis.Pathogens (Basel, Switzerland) · 2023Article
- On the origin of amphi-enterobactin fragments produced by Vibrio campbellii species.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Article
- Recent Advances in the Siderophore Biology ofFrontiers in microbiology · 2022Review
- Structural insights into a novel family of integral membrane siderophore reductases.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The Esterase PfeE, the Achilles' Heel in the Battle for Iron betweenInternational journal of molecular sciences · 2021Article
- Metal homeostasis in pathogenic Epsilonproteobacteria: mechanisms of acquisition, efflux, and regulation.Metallomics : integrated biometal science · 2021Review
- Evaluation of the Immunogenic Response of a Novel Enterobactin Conjugate Vaccine in Chickens for the Production of Enterobactin-Specific Egg Yolk Antibodies.Frontiers in immunology · 2021Article
- The Pneumococcal Iron Uptake Protein A (PiuA) Specifically Recognizes Tetradentate FeJournal of molecular biology · 2020Article
- Iron Acquisition by Bacterial Pathogens: Beyond Tris-Catecholate Complexes.Chembiochem : a European journal of chemical biology · 2020Review
- Enterobactin-Specific Antibodies Induced by a Novel Enterobactin Conjugate Vaccine.Applied and environmental microbiology · 2019Article
- A Cotransformation Method To Identify a Restriction-Modification Enzyme That Reduces Conjugation Efficiency in Campylobacter jejuni.Applied and environmental microbiology · 2018Article
- Design, solid-phase synthesis and evaluation of enterobactin analogs for iron delivery into the human pathogen Campylobacter jejuni.Bioorganic & medicinal chemistry · 2018Article
- Interactions of the periplasmic binding protein CeuE with Fe(III) n-LICAMScientific reports · 2017Article
- Iron Acquisition Mechanisms and Their Role in the Virulence ofFrontiers in cellular and infection microbiology · 2017Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Ferric enterobactin (FeEnt) acquisition is a highly efficient and conserved iron scavenging system in Gram-negative bacteria. Recently, we have characterized two FeEnt receptors (CfrA and CfrB) in Campylobacter jejuni and C. coli, the enteric human pathogens that do not produce any siderophores. In this study, whole-genome sequencing and comparative genomic analysis identified a unique Ent trilactone esterase Cee (Cj1376) in C. jejuni. Genomic analysis and biochemical assay strongly suggested that Cee is the sole trilactone esterase in C. jejuni. Thin-layer chromatography and HPLC analyses showed high efficiency of the purified Cee to hydrolyse Ent. Three Cee homologues previously characterized from other bacteria (IroE, IroD and Fes) were also purified and analysed together with Cee, indicating that Cee, Fes and IroD displayed similar hydrolysis dynamics for both apo and ferric forms of Ent while IroE catalysed Ent inefficiently. Unlike cytoplasmic Fes and IroD, Cee is localized in the periplasm as demonstrated by immunoblotting using Cee-specific antibodies. Genetic manipulation of diverse Campylobacter strains demonstrated that Cee is not only essential for CfrB-dependent FeEnt acquisition but also involved in CfrA-dependent pathway. Together, this study identified and characterized a novel periplasmic trilactone esterase and suggested a new model of FeEnt acquisition in Campylobacter.
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