ArticleMetallomics : integrated biometal science2009
Hijacking transferrin bound iron: protein-receptor interactions involved in iron transport in N. gonorrhoeae.
Article in Metallomics : integrated biometal science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 35 citations in OpenAlex.
- Structural and functional insights into iron acquisition from lactoferrin and transferrin in Gram-negative bacterial pathogens.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023Article
- Extraintestinal PathogenicMicrobiology spectrum · 2022Article
- Reciprocal adaptation of rice and Xanthomonas oryzae pv. oryzae: cross-species 2D GWAS reveals the underlying genetics.The Plant cell · 2021Article
- The Role of theFrontiers in microbiology · 2021Article
- Enteropathogenic Escherichia coli remodels host endosomes to promote endocytic turnover and breakdown of surface polarity.PLoS pathogens · 2019Article
- Transition metals at the host-pathogen interface: howEssays in biochemistry · 2017Review
- Structure of the bacterial plant-ferredoxin receptor FusA.Nature communications · 2016Article
- From Constructs to Crystals - Towards Structure Determination of β-barrel Outer Membrane Proteins.Journal of visualized experiments : JoVE · 2016Article
- Bordetella pertussis FbpA binds both unchelated iron and iron siderophore complexes.Biochemistry · 2014Article
- False-positive rate determination of protein target discovery using a covalent modification- and mass spectrometry-based proteomics platform.Journal of the American Society for Mass Spectrometry · 2014Article
- Structural insight into the lactoferrin receptors from pathogenic Neisseria.Journal of structural biology · 2013Article
- Iron metabolism in aerobes: managing ferric iron hydrolysis and ferrous iron autoxidation.Coordination chemistry reviews · 2013Article
- Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humans.Frontiers in cellular and infection microbiology · 2013Review
- The transferrin-iron import system from pathogenic Neisseria species.Molecular microbiology · 2012Review
- Evidence of Fe3+ interaction with the plug domain of the outer membrane transferrin receptor protein of Neisseria gonorrhoeae: implications for Fe transport.Metallomics : integrated biometal science · 2012Article
- Ferredoxin containing bacteriocins suggest a novel mechanism of iron uptake in Pectobacterium spp.PloS one · 2012Article
- Conserved interaction between transferrin and transferrin-binding proteins from porcine pathogens.The Journal of biological chemistry · 2011Article
- TonB-Dependent Transporters Expressed by Neisseria gonorrhoeae.Frontiers in microbiology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Neisseria gonorrhoeae has the capacity to acquire iron from its human host by removing this essential nutrient from serum transferrin. The transferrin binding proteins, TbpA and TbpB constitute the outer membrane receptor complex responsible for binding transferrin, extracting the tightly bound iron from the host-derived molecule, and transporting iron into the periplasmic space of this Gram-negative bacterium. Once iron is transported across the outer membrane, ferric binding protein A (FbpA) moves the iron across the periplasmic space and initiates the process of transport into the bacterial cytosol. The results of the studies reported here define the multiple steps in the iron transport process in which TbpA and TbpB participate. Using the SUPREX technique for assessing the thermodynamic stability of protein-ligand complexes, we report herein the first direct measurement of periplasmic FbpA binding to the outer membrane protein TbpA. We also show that TbpA discriminates between apo- and holo-FbpA; i.e. the TbpA interaction with apo-FbpA is higher affinity than the TbpA interaction with holo-FbpA. Further, we demonstrate that both TbpA and TbpB individually can deferrate transferrin and ferrate FbpA without energy supplied from TonB resulting in sequestration by apo-FbpA.
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What OpenQuestion holds
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.