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Journal of Bacteriology, June 2009, p. 3901-3908, Vol. 191, No. 12
0021-9193/09/$08.00+0     doi:10.1128/JB.00143-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Characterization of Two Homologous Disulfide Bond Systems Involved in Virulence Factor Biogenesis in Uropathogenic Escherichia coli CFT073{triangledown} ,{dagger}

Makrina Totsika,1 Begoña Heras,2 Daniël J. Wurpel,1 and Mark A. Schembri1*

School of Chemistry and Molecular Biosciences,1 Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia2

Received 2 February 2009/ Accepted 11 April 2009

Disulfide bond (DSB) formation is catalyzed by disulfide bond proteins and is critical for the proper folding and functioning of secreted and membrane-associated bacterial proteins. Uropathogenic Escherichia coli (UPEC) strains possess two paralogous disulfide bond systems: the well-characterized DsbAB system and the recently described DsbLI system. In the DsbAB system, the highly oxidizing DsbA protein introduces disulfide bonds into unfolded polypeptides by donating its redox-active disulfide and is in turn reoxidized by DsbB. DsbA has broad substrate specificity and reacts readily with reduced unfolded proteins entering the periplasm. The DsbLI system also comprises a functional redox pair; however, DsbL catalyzes the specific oxidative folding of the large periplasmic enzyme arylsulfate sulfotransferase (ASST). In this study, we characterized the DsbLI system of the prototypic UPEC strain CFT073 and examined the contributions of the DsbAB and DsbLI systems to the production of functional flagella as well as type 1 and P fimbriae. The DsbLI system was able to catalyze disulfide bond formation in several well-defined DsbA targets when provided in trans on a multicopy plasmid. In a mouse urinary tract infection model, the isogenic dsbAB deletion mutant of CFT073 was severely attenuated, while deletion of dsbLI or assT did not affect colonization.

* Corresponding author. Mailing address: School of Chemistry and Molecular Biosciences, Building 76, University of Queensland, Brisbane, Queensland 4072, Australia. Phone: 617 33653306. Fax: 617 33654699. E-mail: m.schembri{at}uq.edu.au

{triangledown} Published ahead of print on 17 April 2009.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.

Journal of Bacteriology, June 2009, p. 3901-3908, Vol. 191, No. 12
0021-9193/09/$08.00+0     doi:10.1128/JB.00143-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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