ArticleFEMS microbiology letters2013
Specific TonB-ExbB-ExbD energy transduction systems required for ferric enterobactin acquisition in Campylobacter.
Article in FEMS microbiology letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 23 citations in OpenAlex.
- Unraveling aerotolerancy of campylobacter jejuni and campylobacter coli using a transcriptomic approach.Scientific reports · 2026Article
- Transcriptome analysis of aerotolerant and aerosensitiveFrontiers in microbiology · 2025Article
- Uropathogenic Escherichia coli wield enterobactin-derived catabolites as siderophores.The Journal of biological chemistry · 2024Article
- UropathogenicbioRxiv : the preprint server for biology · 2023Article
- Genomic Modification of TonB and Emergence of Small-Colony Phenotype in VIM- and NDM-Producing Escherichia coli following Cefiderocol ExposureAntimicrobial agents and chemotherapy · 2023Article
- Deletion of theFrontiers in veterinary science · 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
- Review on Stress Tolerance inFrontiers in cellular and infection microbiology · 2020Review
- Article
- A Cotransformation Method To Identify a Restriction-Modification Enzyme That Reduces Conjugation Efficiency in Campylobacter jejuni.Applied and environmental microbiology · 2018Article
- The Role of the Regulator Fur in Gene Regulation and Virulence ofFrontiers in cellular and infection microbiology · 2017Article
- Adhesion, Biofilm Formation, and Genomic Features of Campylobacter jejuni Bf, an Atypical Strain Able to Grow under Aerobic Conditions.Frontiers in microbiology · 2016Article
- Article
- Heat Shock-Enhanced Conjugation Efficiency in Standard Campylobacter jejuni Strains.Applied and environmental microbiology · 2015Article
- Analysis of the activity and regulon of the two-component regulatory system composed by Cjj81176_1484 and Cjj81176_1483 of Campylobacter jejuni.Journal of bacteriology · 2015Article
- Important Role of a Putative Lytic Transglycosylase Cj0843c in β-Lactam Resistance in Campylobacter jejuni.Frontiers in microbiology · 2015Article
- TonB Energy Transduction Systems of Riemerella anatipestifer Are Required for Iron and Hemin Utilization.PloS one · 2015Article
- Defining the metabolic requirements for the growth and colonization capacity of Campylobacter jejuni.Frontiers in cellular and infection microbiology · 2014Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
Ferric enterobactin (FeEnt) acquisition plays a critical role in the pathophysiology of Campylobacter, the leading bacterial cause of human gastroenteritis in industrialized countries. In Campylobacter, the surface-exposed receptor, CfrA or CfrB, functions as a 'gatekeeper' for initial binding of FeEnt. Subsequent transport across the outer membrane is energized by TonB-ExbB-ExbD energy transduction systems. Although there are up to three TonB-ExbB-ExbD systems in Campylobacter, the cognate components of TonB-ExbB-ExbD for FeEnt acquisition are still largely unknown. In this study, we addressed this issue using complementary molecular approaches: comparative genomic analysis, random transposon mutagenesis and site-directed mutagenesis in two representative C. jejuni strains, NCTC 11168 and 81-176. We demonstrated that CfrB could interact with either TonB2 or TonB3 for efficient Ent-mediated iron acquisition. However, TonB3 is a dominant player in the CfrA-dependent pathway. The ExbB2 and ExbD2 components were essential for both CfrA- and CfrB-dependent FeEnt acquisition. Sequences analysis identified potential TonB boxes in CfrA and CfrB, and the corresponding binding sites in TonB. In conclusion, these findings identify specific TonB-ExbB-ExbD energy transduction components required for FeEnt acquisition, and provide insights into the complex molecular interactions of FeEnt acquisition systems in Campylobacter.
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Registered trials
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