scholarly journals Characterization of a Gene Encoding the Outer Membrane Receptor for Ferric Enterobactin in Aeromonas hydrophila ATCC 7966T

2013 ◽  
Vol 77 (2) ◽  
pp. 353-360 ◽  
Author(s):  
Tatsuya FUNAHASHI ◽  
Tomotaka TANABE ◽  
Katsushiro MIYAMOTO ◽  
Hiroshi TSUJIBO ◽  
Jun MAKI ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Aeromonas Hydrophila ◽  
Membrane Receptor ◽  
Outer Membrane Receptor ◽  
Gene Encoding

scholarly journals Identification and characterization of an iron-regulated gene, chtA, required for the utilization of the xenosiderophores aerobactin, rhizobactin 1021 and schizokinen by Pseudomonas aeruginosa

Microbiology ◽  
2006 ◽  
Vol 152 (4) ◽  
pp. 945-954 ◽  
Author(s):  
Páraic Ó Cuív ◽  
Paul Clarke ◽  
Michael O'Connell
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Outer Membrane ◽  
Membrane Receptor ◽  
Outer Membrane Receptor ◽  
Significant Similarity ◽  
Hydroxamate Siderophores ◽  
Insertional Inactivation ◽  
Titration Assay

Pseudomonas aeruginosa utilizes several xenosiderophores under conditions of iron limitation, including the citrate hydroxamate siderophore aerobactin. Analysis of the P. aeruginosa genome sequence revealed the presence of two genes, chtA (PA4675) and PA1365, encoding proteins displaying significant similarity to the aerobactin outer-membrane receptor, IutA, of Escherichia coli. The chtA and PA1365 genes were mutated by insertional inactivation and it was demonstrated that ChtA is the outer-membrane receptor for aerobactin. ChtA also mediated the utilization of rhizobactin 1021 and schizokinen, which are structurally similar to aerobactin. In contrast to the utilization of other xenosiderophores by P. aeruginosa, there was no apparent redundancy in the utilization of aerobactin, rhizobactin 1021 and schizokinen. The utilization of citrate hydroxamate siderophores by P. aeruginosa was demonstrated to be TonB1 dependent. A Fur box was identified in the region directly upstream of chtA and it was demonstrated by the in vivo Fur titration assay that this region is capable of binding Fur and accordingly that expression of chtA is iron regulated. The PA1365 mutant was unaffected in the utilization of citrate hydroxamate siderophores.

Characterization of the stability functions and inverted repeat structure X3 of the IncFI plasmid ColV2-K94

1986 ◽  
Vol 32 (10) ◽  
pp. 806-813
Author(s):  
Peter C. Weber ◽  
Sunil Palchaudhuri
Keyword(s):  
Outer Membrane ◽  
Inverted Repeat ◽  
Iron Uptake ◽  
Membrane Receptor ◽  
Outer Membrane Receptor ◽  
Plasmid Maintenance ◽  
Stability Functions ◽  
Repeat Structure ◽  
The Stability

A region of the IncFI plasmid ColV2-K94 which showed homology to the sop partitioning genes of F was cloned and characterized in an attempt to study the stability functions of this element. The sop region contained the incD incompatibility determinant common to many IncFI plasmids, but could not confer on ColV2-K94 miniplasmids the same stable inheritance found in the intact ColV2-K94; thus, other functions appear to be required for efficient plasmid maintenance. Adjacent to the area of sop homology was the X3 region, which was found to contain three inverted IS1-like sequences. The X3 region of ColV2-K94 was similar in organization to the aerobactin iron uptake region of ColV3-K30, but ColV2-K94 lacked the ability to synthesize either the aerobactin siderophore or its outer membrane receptor.

scholarly journals Importance of the Ornibactin and Pyochelin Siderophore Transport Systems in Burkholderia cenocepacia Lung Infections

2004 ◽  
Vol 72 (5) ◽  
pp. 2850-2857 ◽  
Author(s):  
M. B. Visser ◽  
S. Majumdar ◽  
E. Hani ◽  
P. A. Sokol
Keyword(s):  
Salicylic Acid ◽  
Outer Membrane ◽  
Parent Strain ◽  
Membrane Receptor ◽  
Burkholderia Cenocepacia ◽  
Transport Systems ◽  
Uptake System ◽  
Outer Membrane Receptor ◽  
Gene Encoding ◽  
Lung Infections

ABSTRACT Previously, orbA, the gene encoding the outer membrane receptor for ferric-ornibactin, was identified in Burkholderia cenocepacia K56-2, a strain which produces ornibactin, salicylic acid, and negligible amounts of pyochelin. A K56-2 orbA mutant was less virulent than the parent strain in a rat agar bead infection model. In this study, an orbA mutant of B. cenocepacia Pc715j which produces pyochelin in addition to ornibactin and salicylic acid was constructed. The gene encoding the outer membrane receptor for ferric-pyochelin (fptA) was also identified. An fptA mutant was constructed in Pc715j and shown to be deficient in [59Fe]pyochelin uptake. A 75-kDa iron-regulated protein was identified in outer membrane preparations of Pc715j that was absent in outer membrane preparations of Pc715jfptA::tp. Pc715jfptA::tp and Pc715jorbA::tp produced smaller amounts of their corresponding siderophores. Both Pc715jorbA::tp and Pc715jfptA::tp were able to grow in iron starvation conditions in vitro. In the agar bead model, the Pc715jorbA::tp mutant was cleared from the lung, indicating that the pyochelin uptake system does not compensate for the absence of a functional ornibactin system. Pc715jfptA::tp persisted in rat lung infections in numbers similar to those of the parent strain, indicating that the ferric-ornibactin uptake system could compensate for the defect in ferric-pyochelin uptake in vivo. These studies suggest that the ornibactin uptake system is the most important siderophore-mediated iron transport system in B. cenocepacia lung infections.

Characterization of the cloacin DF13/aerobactin outer membrane receptor protein of Escherichia coli (pFS8)

1985 ◽  
Vol 51 (5-6) ◽  
pp. 553-554
Author(s):  
Willy J. A. Krone ◽  
Freek Stegehuis ◽  
Frits K. de Graaf ◽  
Bauke Oudega
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Membrane Receptor ◽  
Receptor Protein ◽  
Outer Membrane Receptor
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