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Infection and Immunity, January 2005, p. 135-145, Vol. 73, No. 1
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.1.135-145.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Molecular Aspects of Biogenesis of Escherichia coli Dr Fimbriae: Characterization of DraB-DraE Complexes

Rafal Piatek,1 Beata Zalewska,1 Olga Kolaj,1 Michal Ferens,1 Bogdan Nowicki,2,3 and Józef Kur1*

Department of Microbiology, Gdansk University of Technology, Gdansk, Poland,1 Department of Obstetrics and Gynecology,2 Department of Microbiology and Immunology, The University of Texas Medical Branch, Galveston, Texas3

Received 30 April 2004/ Returned for modification 17 August 2004/ Accepted 20 September 2004

The Dr hemagglutinin of uropathogenic Escherichia coli is a fimbrial homopolymer of DraE subunits encoded by the dra operon. The dra operon includes the draB and draC genes, whose products exhibit homology to chaperone-usher proteins involved in the biogenesis of surface-located polymeric structures. DraB is one of the periplasmic proteins belonging to the superfamily of PapD-like chaperones. It possesses two conserved cysteine residues characteristic of the FGL subfamily of Caf1M-like chaperones. In this study we obtained evidence that DraB cysteines form a disulfide bond in a mature chaperone and have the crucial function of forming the DraB-DraE binary complex. Expression experiments showed that the DraB protein is indispensable in the folding of the DraE subunit to a form capable of polymerization. Accumulation of DraB-DraEn oligomers, composed of head-to-tail subunits and the chaperone DraB, was observed in the periplasm of a recombinant E. coli strain which expressed DraB and DraE (but not DraC). To investigate the donor strand exchange mechanism during the formation of DraE oligomers, we constructed a series of DraE N-terminal deletion mutants. Deletion of the first three N-terminal residues of a potential donor strand resulted in a DraE protein lacking an oligomerization function. In vitro data showed that the DraE disulfide bond was not needed to form a binary complex with the DraB chaperone but was essential in the polymerization process. Our data suggest that assembly of Dr fimbriae requires a chaperone-usher pathway and the donor strand exchange mechanism.

* Corresponding author. Mailing address: Department of Microbiology, Gdansk University of Technology, ul. Narutowicza 11/12, 80-952 Gdansk, Poland. Phone: 48 58 3471822. Fax: 48 3471822. E-mail: kur{at}altis.chem.pg.gda.pl.

Editor: V. J. DiRita

Infection and Immunity, January 2005, p. 135-145, Vol. 73, No. 1
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.1.135-145.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Zalewska-Piatek, B., Bury, K., Piatek, R., Bruzdziak, P., Kur, J. (2008). Type II Secretory Pathway for Surface Secretion of DraD Invasin from the Uropathogenic Escherichia coli Dr+ Strain. J. Bacteriol. 190: 5044-5056 [Abstract] [Full Text]  
  • Jacobsen, S. M., Stickler, D. J., Mobley, H. L. T., Shirtliff, M. E. (2008). Complicated Catheter-Associated Urinary Tract Infections Due to Escherichia coli and Proteus mirabilis. Clin. Microbiol. Rev. 21: 26-59 [Abstract] [Full Text]  
  • Nuccio, S.-P., Baumler, A. J. (2007). Evolution of the Chaperone/Usher Assembly Pathway: Fimbrial Classification Goes Greek. Microbiol. Mol. Biol. Rev. 71: 551-575 [Abstract] [Full Text]  
  • Zalewska, B., Piatek, R., Bury, K., Samet, A., Nowicki, B., Nowicki, S., Kur, J. (2005). A surface-exposed DraD protein of uropathogenic Escherichia coli bearing Dr fimbriae may be expressed and secreted independently from DraC usher and DraE adhesin. Microbiology 151: 2477-2486 [Abstract] [Full Text]  


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