Outer membrane protein profiles and multilocus enzyme electrophoresis analysis for differentiation of clinical isolates of Proteus mirabilis and Proteus vulgaris.

1992 ◽  
Vol 30 (10) ◽  
pp. 2632-2637 ◽  
Author(s):  
T Kappos ◽  
M A John ◽  
Z Hussain ◽  
M A Valvano
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Proteus Mirabilis ◽  
Clinical Isolates ◽  
Enzyme Electrophoresis ◽  
Protein Profiles ◽  
Proteus Vulgaris ◽  
Multilocus Enzyme Electrophoresis

scholarly journals Identification of a Siderophore Receptor Required for Ferric Ornibactin Uptake in Burkholderia cepacia

2000 ◽  
Vol 68 (12) ◽  
pp. 6554-6560 ◽  
Author(s):  
P. A. Sokol ◽  
P. Darling ◽  
S. Lewenza ◽  
C. R. Corbett ◽  
C. D. Kooi
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Burkholderia Cepacia ◽  
Parent Strain ◽  
Respiratory Infections ◽  
Infection Model ◽  
Protein Profiles ◽  
Outer Membrane Receptor ◽  
Gene Encoding

ABSTRACT Ornibactins are linear hydroxamate siderophores produced byBurkholderia cepacia with peptide structures similar to that of pyoverdines produced by the fluorescent pseudomonads. The gene encoding the outer membrane receptor (orbA) was identified, sequenced, and demonstrated to have significant homology with hydroxamate receptors produced by other organisms. The orbAprecursor was predicted to be a protein with a molecular mass of 81 kDa. An orbA mutant was constructed and demonstrated to be unable to take up 59Fe-ornibactins or to grow in medium supplemented with ornibactins. Outer membrane protein profiles from the parent strain, K56-2, revealed an iron-regulated outer membrane protein of 78 kDa that was not detectable in the K56orbA::tp mutant. When this mutant harbored a plasmid containing the orbA gene, the 78-kDa protein was present in the outer membrane protein profiles and the mutant was able to utilize ornibactin to acquire iron. The orbA mutant was less virulent in a chronic respiratory infection model than the parent strain, indicating that ornibactin uptake and utilization are important in the pathogenesis of B. cepacia respiratory infections.

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