title: Characterization of ferric and ferrous iron transport systems in Vibrio cholerae.
abstract: Vibrio cholerae has multiple iron acquisition systems, including TonB-dependent transport of heme and of the catechol siderophore vibriobactin. Strains defective in both of these systems grow well in laboratory media and in the infant mouse intestine, indicating the presence of additional iron acquisition systems. Previously uncharacterized potential iron transport systems, including a homologue of the ferrous transporter Feo and a periplasmic binding protein-dependent ATP binding cassette (ABC) transport system, termed Fbp, were identified in the V. cholerae genome sequence. Clones encoding either the Feo or the Fbp system exhibited characteristics of iron transporters: both repressed the expression of lacZ cloned under the control of a Fur-regulated promoter in Escherichia coli and also conferred growth on a Shigella flexneri mutant that has a severe defect in iron transport. Two other ABC transporters were also evaluated but were negative by these assays. Transport of radioactive iron by the Feo system into the S. flexneri iron transport mutant was stimulated by the reducing agent ascorbate, consistent with Feo functioning as a ferrous transporter. Conversely, ascorbate inhibited transport by the Fbp system, suggesting that it transports ferric iron. The growth of V. cholerae strains carrying mutations in one or more of the potential iron transport genes indicated that both Feo and Fbp contribute to iron acquisition. However, a mutant defective in the vibriobactin, Fbp, and Feo systems was not attenuated in a suckling mouse model, suggesting that at least one other iron transport system can be used in vivo.
authors.affiliation: University of Texas, Section of Molecular Genetics and Microbiology, 1 University Station A5000, Austin, TX 78712-0162, USA. ewyckoff@mail.utexas.edu
authors.forename: Elizabeth E
authors.initials: EE
authors.lastname: Wyckoff
authors.forename: Alexandra R
authors.initials: AR
authors.lastname: Mey
authors.forename: Andreas
authors.initials: A
authors.lastname: Leimbach
authors.forename: Carolyn F
authors.initials: CF
authors.lastname: Fisher
authors.forename: Shelley M
authors.initials: SM
authors.lastname: Payne
mesh_terms: D018528:ATP-Binding Cassette Transporters; D000818:Animals; D019677:Artificial Gene Fusion; D001205:Ascorbic Acid / Q000737:chemistry; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D001692:Biological Transport / Q000235:genetics; D002396:Catechols; D002771:Cholera / Q000382:microbiology; D004195:Disease Models, Animal; D004926:Escherichia coli / Q000235:genetics; D029968:Escherichia coli Proteins / Q000235:genetics; D005290:Ferric Compounds / Q000378:metabolism*; D005296:Ferrous Compounds / Q000378:metabolism*; D017353:Gene Deletion; D017930:Genes, Reporter; D005816:Genetic Complementation Test; D026901:Membrane Transport Proteins / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D010080:Oxazoles; D010084:Oxidation-Reduction; D011401:Promoter Regions, Genetic; D012763:Shigella flexneri / Q000235:genetics; D014734:Vibrio cholerae / Q000235:genetics / Q000378:metabolism* / Q000472:pathogenicity; D014774:Virulence; D037521:Virulence Factors / Q000235:genetics; D001616:beta-Galactosidase / Q000096:biosynthesis / Q000235:genetics
chemical_list: D018528:ATP-Binding Cassette Transporters; D001426:Bacterial Proteins; D002396:Catechols; D029968:Escherichia coli Proteins; D005290:Ferric Compounds; D005296:Ferrous Compounds; D026901:Membrane Transport Proteins; D010080:Oxazoles; D037521:Virulence Factors; C100775:feo protein, E coli; C040227:vibriobactin; D001616:beta-Galactosidase; D001205:Ascorbic Acid