Effect of the crp mutation on the utilization of transferrin-bound iron by Vibrio vulnificus
Autor: | Sung-Heui Shin, Ra-Young Park, Choon-Mee Kim, Young Ran Kim, Hui-Yu Sun, Joon Haeng Rhee, Mi-Hwa Choi, Young-Hoon Bai |
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Rok vydání: | 2006 |
Předmět: |
Iron
Mutant Molecular Sequence Data Virulence Down-Regulation Siderophores Vibrio vulnificus Biology Microbiology Receptors Cyclic AMP Bacterial Proteins Genetics Ascitic Fluid Humans Receptor Molecular Biology Gene Oxazoles chemistry.chemical_classification Base Sequence Transferrin biology.organism_classification Amides Culture Media Complementation Repressor Proteins chemistry Regulatory sequence Mutation Bacterial Outer Membrane Proteins |
Zdroj: | FEMS microbiology letters. 257(2) |
ISSN: | 0378-1097 |
Popis: | Cyclic AMP-cAMP receptor protein (CRP) complex plays an essential role in the global regulation of Vibrio vulnificus virulence. We found that growth retardation of V. vulnificus caused by mutation of the crp gene encoding CRP was exacerbated under iron-limited conditions. Accordingly, we investigated the effect of crp mutation on the expression of the vulnibactin-mediated iron-uptake system and the ability of V. vulnificus to utilize transferrin-bound iron, and thus to grow in cirrhotic ascites, a human ex vivo system. The production of vulnibactin was suppressed, and the transcription of the vis and vuuA genes, which encode an enzyme required for vulnibactin synthesis and vulnibactin receptor protein, was also suppressed in the crp mutant. Moreover, the crp mutant could not utilize transferrin-bound iron, and its growth was severely suppressed both on transferrin-bound iron and in cirrhotic ascites. All the defects in the crp mutant were recovered by the in trans complementation of the wild-type crp gene. Putative CRP-binding sequences were found in the regulatory regions of the fur, vis and vuuA genes. These results indicate that crp mutation attenuates the ability to grow on transferrin-bound iron and in a human body fluid by down-regulating the vulnibactin-mediated iron-uptake system. |
Databáze: | OpenAIRE |
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