| Energy-dependent changes in the gonococcal transferrin receptor. | |
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MedLine Citation:
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PMID: 9383187 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The pathogenic Neisseria spp. are capable of iron utilization from host iron-binding proteins including transferrin and lactoferrin. Transferrin iron utilization is an energy-dependent, receptor-mediated event in which two identified transferrin-binding proteins participate. One of these proteins, TbpA, is homologous to the TonB-dependent family of outer membrane receptors that are required for high-affinity uptake of vitamin B12 and ferric siderophores. The 'TonB box' is a conserved domain near the amino-terminus of these proteins that has been implicated in interaction with TonB. Interaction between a periplasmic domain of TonB and the TonB box allows energy transduction to occur from the cytoplasmic membrane to the energy-dependent receptor in the outer membrane. We created a TonB box mutant of gonococcal TbpA and demonstrated that its binding and protease accessibility characteristics were indistinguishable from those of gonococcal Ton system mutants. The protease exposure of the second transferrin-binding protein, TbpB, was affected by the energization of TbpA, consistent with an interaction between these proteins. TbpB expressed by the de-energized mutants was readily accessible to protease, similar to TbpB expressed in the absence of TbpA. The de-energized mutants exhibited a marked decrease in transferrin diffusion rate, suggesting that receptor energization was necessary for ligand release. We propose a model to explain the observed Ton-dependent changes in the binding parameters and exposures of TbpA and TbpB. |
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Authors:
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C N Cornelissen; J E Anderson; P F Sparling |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Molecular microbiology Volume: 26 ISSN: 0950-382X ISO Abbreviation: Mol. Microbiol. Publication Date: 1997 Oct |
Date Detail:
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Created Date: 1998-01-27 Completed Date: 1998-01-27 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 8712028 Medline TA: Mol Microbiol Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 25-35 Citation Subset: IM |
Affiliation:
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Department of Medicine, School of Medicine, University of North Carolina at Chapel Hill, USA. ccornelissen@gems.vcu.edu |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Bacterial Outer Membrane Proteins
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genetics,
metabolism Bacterial Proteins / genetics, metabolism* Blotting, Western Carrier Proteins / genetics, metabolism* Energy Metabolism Iron / metabolism* Iron-Binding Proteins Kinetics Membrane Proteins / genetics, metabolism* Models, Molecular Mutagenesis, Site-Directed Neisseria gonorrhoeae / chemistry, genetics, metabolism* Protein Binding Protein Conformation Receptors, Transferrin / chemistry, metabolism* Transferrin / metabolism Transferrin-Binding Proteins Trypsin / metabolism |
| Grant Support | |
ID/Acronym/Agency:
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AI26837/AI/NIAID NIH HHS; AI31496/AI/NIAID NIH HHS; AI39523/AI/NIAID NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Outer Membrane Proteins; 0/Bacterial Proteins; 0/Carrier Proteins; 0/Iron-Binding Proteins; 0/Membrane Proteins; 0/Receptors, Transferrin; 0/Transferrin-Binding Proteins; 0/tonB protein, Bacteria; 11096-37-0/Transferrin; 7439-89-6/Iron; EC 3.4.21.4/Trypsin |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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