title: Nonredundant Roles of Iron Acquisition Systems in Vibrio cholerae.
abstract: Vibrio cholerae, the causative agent of the severe diarrheal disease cholera, thrives in both marine environments and the human host. To do so, it must encode the tools necessary to acquire essential nutrients, including iron, under these vastly different conditions. A number of V. cholerae iron acquisition systems have been identified; however, the precise role of each system is not fully understood. To test the roles of individual systems, we generated a series of mutants in which only one of the four systems that support iron acquisition on unsupplemented LB agar, Feo, Fbp, Vct, and Vib, remains functional. Analysis of these mutants under different growth conditions showed that these systems are not redundant. The strain carrying only the ferrous iron transporter Feo grew well at acidic, but not alkaline, pH, whereas the ferric iron transporter Fbp promoted better growth at alkaline than at acidic pH. A strain defective in all four systems (null mutant) had a severe growth defect under aerobic conditions but accumulated iron and grew as well as the wild type in the absence of oxygen, suggesting the presence of an additional, unidentified iron transporter in V. cholerae. In support of this, the null mutant was only moderately attenuated in an infant mouse model of infection. While the null mutant used heme as an iron source in vitro, we demonstrate that heme is not available to V. cholerae in the infant mouse intestine.
authors.affiliation: Department of Molecular Biosciences, The University of Texas, Austin, Texas, USA.
authors.forename: Eric D
authors.initials: ED
authors.lastname: Peng
authors.affiliation: Department of Molecular Biosciences, The University of Texas, Austin, Texas, USA.
authors.forename: Elizabeth E
authors.initials: EE
authors.lastname: Wyckoff
authors.affiliation: Department of Molecular Biosciences, The University of Texas, Austin, Texas, USA.
authors.forename: Alexandra R
authors.initials: AR
authors.lastname: Mey
authors.affiliation: Department of Molecular Biosciences, The University of Texas, Austin, Texas, USA.
authors.forename: Carolyn R
authors.initials: CR
authors.lastname: Fisher
authors.affiliation: Department of Molecular Biosciences, The University of Texas, Austin, Texas, USA smpayne@austin.utexas.edu.
authors.forename: Shelley M
authors.initials: SM
authors.lastname: Payne
mesh_terms: D000818:Animals; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D002771:Cholera / Q000378:metabolism / Q000382:microbiology*; D004195:Disease Models, Animal; D006418:Heme / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007413:Intestinal Mucosa / Q000378:metabolism; D007422:Intestines / Q000382:microbiology; D007501:Iron / Q000378:metabolism*; D051379:Mice; D009154:Mutation; D010100:Oxygen / Q000378:metabolism; D010453:Peptide Synthases / Q000235:genetics / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000235:genetics / Q000378:metabolism; D014734:Vibrio cholerae / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D011956:Receptors, Cell Surface; C460862:VctA protein, Vibrio cholerae; D006418:Heme; D007501:Iron; D010453:Peptide Synthases; C405545:VibF protein, bacteria; D010100:Oxygen