Characterization of ferric-anguibactin transport in Vibrio anguillarum

Claudia S. López, Jorge H. Crosa

Research output: Contribution to journalArticle

19 Scopus citations

Abstract

The fish pathogen Vibrio anguillarum is the causative agent of a fatal hemorrhagic septicemia in salmonid fish. Many serotype O1 strains harbors a 65 Kbp plasmid (pJM1 encoding an iron sequestering system essential for virulence. The genes involved in the biosynthesis of the indigenous siderophore anguibactin are encoded by both the pJM1 plasmid and the chromosome, while those involved in the transport of the ferric-siderophore complex, including the outer membrane receptor, are plasmid-encoded. This work describes the role of specific amino acid residues of the outer membrane receptor FatA in the mechanism of transport of ferric-anguibactin. FatA modeling indicated that this protein has a 22 stranded β-barrel blocked by the plug domain, the latter being formed by residues 51-154. Deletion of the plug domain resulted in a receptor unable to act as an open channel for the transport of the ferric anguibactin complex.

Original languageEnglish (US)
Pages (from-to)393-403
Number of pages11
JournalBioMetals
Volume20
Issue number3-4
DOIs
StatePublished - Jun 1 2007

Keywords

  • Anguibactin
  • Iron transport
  • Plug domain
  • Receptor
  • TonB2
  • Vibrio anguillarum

ASJC Scopus subject areas

  • Biomaterials
  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)
  • Metals and Alloys

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