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Microbiology 150 (2004), 3657-3667; DOI  10.1099/mic.0.27371-0
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Microbiology 150 (2004), 3657-3667; DOI  10.1099/mic.0.27371-0
© 2004 Society for General Microbiology

The siderophore-mediated iron acquisition systems of Acinetobacter baumannii ATCC 19606 and Vibrio anguillarum 775 are structurally and functionally related

Caleb W. Dorsey1, Andrew P. Tomaras1, Pamela L. Connerly1, Marcelo E. Tolmasky2, Jorge H. Crosa3 and Luis A. Actis1

1 Department of Microbiology, 40 Pearson Hall, Miami University, Oxford, OH 45056, USA
2 Department of Biological Science, California State University Fullerton, Fullerton, CA 92834-6850, USA
3 Department of Molecular Microbiology and Immunology, School of Medicine, Oregon Health Sciences University, Portland, OR 97201-3098, USA

Correspondence
Luis A. Actis
actisla{at}muohio.edu

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.


Abbreviations: ABC, ATP-binding cassette; CAS, Chrome azurol S; DP, 2,2'-dipyridyl; EDDHA, ethylenediamine-di-(o-hydroxyphenyl) acetic acid; HRP, horseradish peroxidase; NTA, nitrilotriacetic acid; TF, human transferrin

The GenBank/EMBL/DDBJ accession number for the sequence of the A. baumannii ATCC 19606 genomic region containing acinetobactin biosynthetic and transport genes is AY571146.




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