Abstract
The pathogenic bacterium Aeromonas hydrophila has been shown to exclusively utilize a ligand exchange mechanism for siderophore-mediated iron uptake, with a single nonspecific siderophore receptor facilitating iron exchange. However, the genes involved in this process, including the gene encoding the nonspecific receptor, are unknown. Here we identify and characterize a novel gene, nsrl, from A. hydrophila that encodes a putative protein with high homology and significant predicted structural similarities to the FhuA protein and other known ferric-siderophore receptors. This protein appears to localize on the cell membrane and is likely to be the receptor involved in the ligand exchange siderophore-mediated iron uptake mechanism of A. hydrophila. It is expected that this information may lead to e development of new antibiotics targeting either nsrl or its gene product for use in controlling A. hydrophila infection.
| Original language | English |
|---|---|
| Pages (from-to) | 31-36 |
| Number of pages | 6 |
| Journal | Drug Target Insights |
| Volume | 2008 |
| Issue number | 3 |
| DOIs | |
| State | Published - 2008 |
Keywords
- Bacterial virulence
- Ferric iron
- Infection
- Iron uptake
- Pathogenecity