Iron is an essential element for bacterial survival and proliferation. However, the availability of iron is extremely limited because it is insoluble in water under aerobic environments and neutral pH or is sequestered in the vertebrate host by the use of high-affinity iron-binding molecules, such as transferrin, lactoferrin, and heme in hemoglobin.1) Most bacteria have accordingly evolved specialized iron acquisition systems to overcome the conditions of its restriction. One of the common strategies for iron acquisition is the use of siderophores, high-affinity ferric iron-chelating molecules.
2)In response to conditions of iron depletion, many bacteria are able not only to biosynthesize and secrete cognate siderophores, but also to pirate siderophores produced by other microbial species (termed xenosiderophores).2) In Gram-negative bacteria, ferric ion trapped with such a siderophore is taken up into cells via the siderophore-specific TonB-dependent outer membrane receptor and ATP binding cassette (ABC) transporter system.3) However, under iron-replete conditions, most of the genes involved in iron acquisition systems are negatively regulated by a ferric uptake regulation (Fur) protein with ferrous iron as a corepressor.
4)Vibrio (V.) furnissii, first described as a gas-producing biogroup of V. fluvialis, was classified by DNA relatedness as a species separate from V. fluvialis. 5) V. furnissii, like other pathogenic Vibrio species, is a halophilic Gram-negative bacterium and is thought to cause acute gastroenteritis and diarrhea through eating seafood contaminated with the bacterium.6) We previously observed that V. furnissii produces the siderophore fluvibactin, which is produced by V. fluvialis, 7) to capture insoluble ferric iron. However, although the ability to use xenosiderophores has been elucidated in some Vibrio species, such as V. vulnificus, 8,9) V. parahaemolyticus, 10,11) and V. cholerae, 12) little is known about that of other Vibrio species including V. furnissii. In this study, we found that V. furnissii can use a fungal siderophore, desferrioxamine B (DFOB), as the iron source. This prompted us to investigate genes involved in the utilization of DFOB by the bacterium. As a result, V. furnissii was found to possess not only a gene (called desA) encoding a TonB-dependent outer membrane receptor protein with an amino acid sequence homologous to the ferrioxamine B (FOB, an ironbound form of DFOB) receptor derived from the V. vulnificus desA gene, 8) but also a gene (called desR), located just upstream of desA, encoding a putative AraC-type transcriptional regulator. The functions of desA and desR that encode the receptor of FOB and the transcriptional activator of desA, respectively, were confirmed by phenotypic analyses of the respective gene-deletion mutants constructed from V. furnissii followed by complementation experiments.
MATERIALS AND METHODS
Bacterial Strains and Media V. furnissii ATCC35016(type strain) isolated from human feces was used in this study. V. furnissii and Escherichia coli...