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

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.

1997 ◽  
Vol 179 (4) ◽  
pp. 1082-1089 ◽  
Author(s):  
J C Fenno ◽  
G W Wong ◽  
P M Hannam ◽  
K H Müller ◽  
W K Leung ◽  
...  

Microbiology ◽  
2010 ◽  
Vol 156 (9) ◽  
pp. 2842-2854 ◽  
Author(s):  
Yih-Yuan Chen ◽  
Chieh-Hao Wu ◽  
Juey-Wen Lin ◽  
Shu-Fen Weng ◽  
Yi-Hsiung Tseng

Xanthomonas campestris pv. campestris (Xcc) is the phytopathogen that causes black rot in crucifers. The xanthan polysaccharide and extracellular enzymes produced by this organism are virulence factors, the expression of which is upregulated by Clp (CRP-like protein) and DSF (diffusible signal factor), which is synthesized by RpfF. It is also known that biofilm formation/dispersal, regulated by the effect of controlled synthesis of DSF on cell–cell signalling, is required for virulence. Furthermore, a deficiency in DSF causes cell aggregation with concomitant production of a gum-like substance that can be dispersed by addition of DSF or digested by exogenous endo-β-1,4-mannanase expressed by Xcc. In this study, Western blotting of proteins from a mopB mutant (XcMopB) showed Xcc MopB to be the major outer-membrane protein (OMP); Xcc MopB shared over 97 % identity with homologues from other members of Xanthomonas. Similarly to the rpfF mutant, XcMopB formed aggregates with simultaneous production of a gummy substance, but these aggregates could not be dispersed by DSF or endo-β-1,4-mannanase, indicating that different mechanisms were involved in aggregation. In addition, XcMopB showed surface deformation, altered OMP composition, impaired xanthan production, increased sensitivity to stressful conditions including SDS, elevated temperature and changes in pH, reduced adhesion and motility and defects in pathogenesis. The finding that the major OMP is required for pathogenicity is unprecedented in phytopathogenic bacteria.


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