has two siderophore-based high-affinity iron-uptake systems utilizing pyoverdin and pyochelin. Using strain IA1, a mutant deficient in production of both siderophores, we have shown that addition of purified siderophore to the growth medium induces expression of specific iron-regulated outer-membrane proteins and increases Fe-siderophore transport. Addition of pyoverdin from the parent strain PAO1 or from a clinical strain 0:12 induced expression of an 85 kDa IROMP and increased the rate of Fe-pyoverdin transport. Transport rates for Fe-PAO1 pyoverdin increased from 1.27 to 3.57 pmol Fe min per 10 cells. Addition of purified pyochelin induced expression of a 75 kDa IROMP accompanied with increased Fe-pyochelin uptake without affecting Fe-pyoverdin transport. Fe-pyochelin transport increased from 0.3 to 10.6 pmol min per 10 cells. Addition of pyoverdin from the parent strain or a chromatographically distinct pyoverdin caused increased reactivity with an anti-85 kDa mAb in Western blotting, indicating that the same receptor is being induced. These results suggest that can respond specifically to the presence of siderophore and moreover that not only can the pyoverdin receptor transport its cognate ferri-pyoverdin but also different ferri-pyoverdins, albeit at a reduced rate.


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