The siderophore-mediated iron acquisition systems of Acinetobacter baumannii ATCC 19606 and Vibrio anguillarum 775 are structurally and functionally related
Open Access
- 1 November 2004
- journal article
- Published by Microbiology Society in Microbiology
- Vol. 150 (11) , 3657-3667
- https://doi.org/10.1099/mic.0.27371-0
Abstract
The Acinetobacter baumannii type strain, ATCC 19606, secretes acinetobactin, a catechol siderophore highly related to the iron chelator anguibactin produced by the fish pathogen Vibrio anguillarum (Listonella anguillarum). This paper reports the initial characterization of the genes and gene products involved in the acinetobactin-mediated iron-acquisition process. Insertional mutagenesis resulted in the isolation of several derivatives whose ability to grow in medium containing the iron chelator 2,2′-dipyridyl was affected. One of the insertions disrupted a gene encoding a predicted outer-membrane protein, named BauA, highly similar to FatA, the receptor for ferric anguibactin. Immunological relatedness of BauA with FatA was confirmed by Western blot analysis. Another transposon insertion was mapped to a gene encoding a protein highly similar to FatD, the permease component of the anguibactin transport system. Further DNA sequencing and nucleotide sequence analysis revealed that these A. baumannii 19606 genes are part of a polycistronic locus that contains the bauDCEBA ORFs. While the translation products of bauD, -C, -B and -A are highly related to the V. anguillarum FatDCBA iron-transport proteins, the product of bauE is related to the ATPase component of Gram-positive ATP-binding cassette (ABC) transport systems. This entire locus is flanked by genes encoding predicted proteins related to AngU and AngN, V. anguillarum proteins required for the biosynthesis of anguibactin. These protein similarities, as well as the structural similarity of anguibactin and acinetobactin, suggested that these two siderophores could be utilized by both bacterial strains, a possibility that was confirmed by siderophore utilization bioassays. Taken together, these results demonstrate that these pathogens, which cause serious infections in unrelated hosts, express very similar siderophore-mediated iron-acquisition systems.Keywords
This publication has 50 references indexed in Scilit:
- Detection and Analysis of Iron Uptake Components Expressed by Acinetobacter baumannii Clinical IsolatesJournal of Clinical Microbiology, 2003
- Genetic and Phenotypic Analysis of Acinetobacter baumannii Insertion Derivatives Generated with a Transposome SystemApplied and Environmental Microbiology, 2002
- Expression of iron binding proteins and hemin binding activity in the dental pathogenActinobacillus actinomycetemcomitansFEMS Microbiology Letters, 1998
- Characterization and regulation of the expression of FatB, an iron transport protein encoded by the pJM1 virulence plasmidMolecular Microbiology, 1995
- An improved system for gene replacement and xylE fusion analysis in Pseudomonas aeruginosaGene, 1995
- A histidine decarboxylase gene encoded by the Vibrio anguillarum plasmid pJM1 is essential for virulence: histamine is a precursor in the biosynthesis of anguibactinMolecular Microbiology, 1995
- Organization of genes encoding membrane proteins of the Escherichia coli ferrienterobactin permeaseMolecular Microbiology, 1991
- Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectorsGene, 1985
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976