Characterization of ferric-anguibactin transport in Vibrio anguillarum

被引:0
|
作者
Claudia S. López
Jorge H. Crosa
机构
[1] Oregon Health and Science University,Department of Molecular Microbiology and Immunology
来源
BioMetals | 2007年 / 20卷
关键词
Iron transport; Anguibactin; Receptor; TonB2; Plug domain;
D O I
暂无
中图分类号
学科分类号
摘要
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 ß-barrel blocked by the plug domain, the latter being formed by residues 51–54. Deletion of the plug domain resulted in a receptor unable to act as an open channel for the transport of the ferric anguibactin complex.
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页码:393 / 403
页数:10
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