Salmochelins, siderophores of Salmonella enterica and uropathogenic Escherichia coli strains, are recognized by the outer membrane receptor IroN
| Autor: | Klaus Hantke, G. Winkelmann, W. Rabsch, G. Nicholson |
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| Rok vydání: | 2003 |
| Předmět: |
Spectrometry
Mass Electrospray Ionization Siderophore Multidisciplinary biology Chemistry Escherichia coli Proteins Iron Cell Membrane Salmonella enterica Siderophores Receptors Cell Surface Siderocalin biology.organism_classification medicine.disease_cause Serine Biochemistry Physical Sciences Glycosyltransferase Escherichia coli medicine biology.protein Moiety Bacterial outer membrane |
| Zdroj: | Proceedings of the National Academy of Sciences. 100:3677-3682 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.0737682100 |
| Popis: | Members of a family of catecholate siderophores, called salmochelins, were isolated by reversed-phase HPLC from Salmonella enterica serotype Typhimurium and structurally characterized by Fourier transform ion cyclotron resonance–MS/MS and GC–MS. The tentative structure of salmochelin 1 contained two 2,3- dihydroxybenzoylserine moieties bridged by a glucose residue, bound to the serine hydroxyl group of one moiety and the carboxylate of the second moiety. Salmochelin 2 contained in addition a second glucose residue linked to a third 2,3-dihydroxybenzoylserine moiety. Salmochelins were not produced by an iroBC mutant, which indicated that the IroB protein might be responsible for the glucosyl transfer predicted by sequence similarities to known glycosyltransferases. Uptake experiments with radiolabeled 55 Fe-salmochelin and growth promotion tests with salmochelins showed that the IroN outer membrane receptor, encoded in the iroA locus of S. enterica and uropathogenic Escherichia coli strains, was the main receptor for ferric salmochelin transport. |
| Databáze: | OpenAIRE |
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