title: Identification of the Vibrio cholerae enterobactin receptors VctA and IrgA: IrgA is not required for virulence.
abstract: The gram-negative enteric pathogen Vibrio cholerae requires iron for growth. V. cholerae has multiple iron acquisition systems, including utilization of heme and hemoglobin, synthesis and transport of the catechol siderophore vibriobactin, and transport of several siderophores that it does not itself make. One siderophore that V. cholerae transports, but does not make, is enterobactin. Enterobactin transport requires TonB and is independent of the vibriobactin receptor ViuA. In this study, two candidate enterobactin receptor genes, irgA (VC0475) and vctA (VCA0232), were identified by analysis of the V. cholerae genomic sequence. A single mutation in either of these genes did not significantly impair enterobactin utilization, but a strain defective in both genes did not use enterobactin. When either irgA or vctA was supplied on a plasmid, the ability of the irgA vctA double mutant to use enterobactin was restored. This indicates that both VctA and IrgA transport enterobactin. We also identify the genes vctPDGC, which are linked to vctA and encode a periplasmic binding protein-dependent ABC transport system that functions in the utilization of both enterobactin and vibriobactin (VCA0227-0230). An irgA::TnphoA mutant strain, MBG40, was shown in a previous study to be highly attenuated and to have a strong colonization defect in an infant mouse model of V. cholerae infection (M. B. Goldberg, V. J. DiRita, and S. B. Calderwood, Infect. Immun. 58:55-60, 1990). In this work, a new irgA mutation was constructed, and this mutant strain was not significantly impaired in its ability to compete with the parental strain in infant mice and was not attenuated for virulence in an assay of 50% lethal dose. These data indicate that the virulence defect in MBG40 is not due to the loss of irgA function and that irgA is unlikely to be an important virulence factor.
authors.affiliation: Institute for Cellular and Molecular Biology, The University of Texas, Austin, Texas 78712-1095, USA.
authors.forename: Alexandra R
authors.initials: AR
authors.lastname: Mey
authors.forename: Elizabeth E
authors.initials: EE
authors.lastname: Wyckoff
authors.forename: Amanda G
authors.initials: AG
authors.lastname: Oglesby
authors.forename: Eva
authors.initials: E
authors.lastname: Rab
authors.forename: Ronald K
authors.initials: RK
authors.lastname: Taylor
authors.forename: Shelley M
authors.initials: SM
authors.lastname: Payne
mesh_terms: D018528:ATP-Binding Cassette Transporters; D000818:Animals; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D001483:Base Sequence; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D002771:Cholera / Q000382:microbiology; D004269:DNA, Bacterial; D004195:Disease Models, Animal; D004758:Enterobactin / Q000378:metabolism*; D051379:Mice; D008807:Mice, Inbred BALB C; D008969:Molecular Sequence Data; D016296:Mutagenesis; D019897:Periplasm / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D014734:Vibrio cholerae / Q000235:genetics / Q000378:metabolism* / Q000472:pathogenicity; D014774:Virulence
chemical_list: D018528:ATP-Binding Cassette Transporters; D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D002352:Carrier Proteins; D004269:DNA, Bacterial; D011956:Receptors, Cell Surface; C460862:VctA protein, Vibrio cholerae; C029489:enterobactin receptor; C074789:irgA protein, Vibrio cholerae; D004758:Enterobactin