Characterization of ferric-anguibactin transport in Vibrio anguillarum

Claudia Lopez, Jorge H. Crosa

Research output: Contribution to journalArticle

19 Citations (Scopus)

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 2007

Fingerprint

Vibrio anguillarum
Vibrio
Fish
Siderophores
plasmids
Plasmids
siderophores
Membranes
receptors
Biosynthesis
Fishes
Hemorrhagic Septicemia
Pathogens
Chromosomes
Ports and harbors
Amino acids
Genes
septicemia
Iron
Proteins

Keywords

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

ASJC Scopus subject areas

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

Cite this

Characterization of ferric-anguibactin transport in Vibrio anguillarum. / Lopez, Claudia; Crosa, Jorge H.

In: BioMetals, Vol. 20, No. 3-4, 06.2007, p. 393-403.

Research output: Contribution to journalArticle

Lopez, Claudia ; Crosa, Jorge H. / Characterization of ferric-anguibactin transport in Vibrio anguillarum. In: BioMetals. 2007 ; Vol. 20, No. 3-4. pp. 393-403.
@article{8ba31b25d62c4a33bf3f8df8a4ab3b6c,
title = "Characterization of ferric-anguibactin transport in Vibrio anguillarum",
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.",
keywords = "Anguibactin, Iron transport, Plug domain, Receptor, TonB2, Vibrio anguillarum",
author = "Claudia Lopez and Crosa, {Jorge H.}",
year = "2007",
month = "6",
doi = "10.1007/s10534-007-9084-9",
language = "English (US)",
volume = "20",
pages = "393--403",
journal = "BioMetals",
issn = "0966-0844",
publisher = "Springer Netherlands",
number = "3-4",

}

TY - JOUR

T1 - Characterization of ferric-anguibactin transport in Vibrio anguillarum

AU - Lopez, Claudia

AU - Crosa, Jorge H.

PY - 2007/6

Y1 - 2007/6

N2 - 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.

AB - 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.

KW - Anguibactin

KW - Iron transport

KW - Plug domain

KW - Receptor

KW - TonB2

KW - Vibrio anguillarum

UR - http://www.scopus.com/inward/record.url?scp=34248664685&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34248664685&partnerID=8YFLogxK

U2 - 10.1007/s10534-007-9084-9

DO - 10.1007/s10534-007-9084-9

M3 - Article

VL - 20

SP - 393

EP - 403

JO - BioMetals

JF - BioMetals

SN - 0966-0844

IS - 3-4

ER -