The high-affinity phosphate transporter Pst in Proteus mirabilis HI4320 and its importance in biofilm formation
The high-affinity phosphate transporter Pst in Proteus mirabilis HI4320 and its importance in biofilm formation
Proteus mirabilis causes urinary tract infections (UTIs) in individuals requiring long-term indwelling catheterization. The pathogenesis of this uropathogen is mediated by a number of virulence factors and the formation of crystalline biofilms. In addition, micro-organisms have evolved complex systems for the acquisition of nutrients, including the phosphate-specific transport system, which has been shown to be important in biofilm formation and pathogenesis. A functional Pst system is important during UTIs caused by P. mirabilis HI4320, since transposon mutants in the PstS periplasmic binding protein and the PstA permease protein were attenuated in the CBA mouse model of UTI. These mutants displayed a defect in biofilm formation when grown in human urine. This study focuses on a comparison of the proteomes during biofilm and planktonic growth in phosphate-rich medium and human urine, and microscopic investigations of biofilms formed by the pst mutants. Our data suggest that (i) the Deltapst mutants, and particularly the DeltapstS mutant, are defective in biofilm formation, and (ii) the proteomes of these mutants differ significantly from that of the wild-type. Therefore, since the Pst system of P. mirabilis HI4320 negatively regulates biofilm formation, this system is important for the pathogenesis of these organisms during complicated UTIs
1523-1535
May, G. A.
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Jacobsen, S.M.
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Longwell, M.
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Stoodley, P.
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Mobley, H.L.T.
d967f084-d0bb-431e-b96f-fcd4b1c18334
Shirtliff, M.E.
aad0fcd1-4fad-4977-afbe-8c1b1844bfbc
May 2009
May, G. A.
e0bc3801-a53c-4e57-bd1e-375353ca0e5d
Jacobsen, S.M.
c0ae8443-bbec-4bbc-b003-76410c30a507
Longwell, M.
37efd2cf-0784-4790-9755-79304d9e48a5
Stoodley, P.
08614665-92a9-4466-806e-20c6daeb483f
Mobley, H.L.T.
d967f084-d0bb-431e-b96f-fcd4b1c18334
Shirtliff, M.E.
aad0fcd1-4fad-4977-afbe-8c1b1844bfbc
May, G. A., Jacobsen, S.M., Longwell, M., Stoodley, P., Mobley, H.L.T. and Shirtliff, M.E.
(2009)
The high-affinity phosphate transporter Pst in Proteus mirabilis HI4320 and its importance in biofilm formation.
Microbiology, 155 (5), .
(doi:10.1099/mic.0.026500-0).
Abstract
Proteus mirabilis causes urinary tract infections (UTIs) in individuals requiring long-term indwelling catheterization. The pathogenesis of this uropathogen is mediated by a number of virulence factors and the formation of crystalline biofilms. In addition, micro-organisms have evolved complex systems for the acquisition of nutrients, including the phosphate-specific transport system, which has been shown to be important in biofilm formation and pathogenesis. A functional Pst system is important during UTIs caused by P. mirabilis HI4320, since transposon mutants in the PstS periplasmic binding protein and the PstA permease protein were attenuated in the CBA mouse model of UTI. These mutants displayed a defect in biofilm formation when grown in human urine. This study focuses on a comparison of the proteomes during biofilm and planktonic growth in phosphate-rich medium and human urine, and microscopic investigations of biofilms formed by the pst mutants. Our data suggest that (i) the Deltapst mutants, and particularly the DeltapstS mutant, are defective in biofilm formation, and (ii) the proteomes of these mutants differ significantly from that of the wild-type. Therefore, since the Pst system of P. mirabilis HI4320 negatively regulates biofilm formation, this system is important for the pathogenesis of these organisms during complicated UTIs
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Published date: May 2009
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The National Centre for Advanced Tribology at Southampton (nCATS)
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Local EPrints ID: 71658
URI: http://eprints.soton.ac.uk/id/eprint/71658
ISSN: 1350-0872
PURE UUID: 28ff9f2a-3651-441c-90fc-f8596ba0c12b
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Date deposited: 17 Dec 2009
Last modified: 14 Mar 2024 02:55
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Author:
G. A. May
Author:
S.M. Jacobsen
Author:
M. Longwell
Author:
H.L.T. Mobley
Author:
M.E. Shirtliff
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