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Infection and Immunity, September 2005, p. 6119-6126, Vol. 73, No. 9
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.9.6119-6126.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Hydrophilic Domain II of Escherichia coli Dr Fimbriae Facilitates Cell Invasion

Margaret Das,1 Audrey Hart-Van Tassell,1 Petri T. Urvil,1 Susan Lea,4 David Pettigrew,4 K. L. Anderson,4 Alfred Samet,6 Jozef Kur,3 Steve Matthews,5 Stella Nowicki,1 Vsevolod Popov,2 Pawel Goluszko,1 and Bogdan J. Nowicki1*

Departments of Obstetrics & Gynecology,1 Pathology, University of Texas Medical Branch, 301 University Blvd., Galveston, Texas 77555-1062,2 Department of Microbiology, Technical University of Gdansk, ul. G. Narutowicza 11/12, 80-952 Gdansk, Poland,3 Department of Biochemistry, Oxford University, Oxford OX1 2QY, United Kingdom,4 Imperial College, London SW 2AZ, United Kingdom,5 Department of Clinical Microbiology, Medical School of Gdansk, Gdansk 80-952, Poland6

Received 21 June 2004/ Returned for modification 7 September 2004/ Accepted 5 April 2005

Uropathogenic and diarrheal Escherichia coli strains expressing adhesins of the Dr family bind to decay-accelerating factor, invade epithelial cells, preferentially infect children and pregnant women, and may be associated with chronic or recurrent infections. Thus far, no fimbrial domain(s) that facilitates cell invasion has been identified. We used alanine scanning mutagenesis to replace selected amino acids in hydrophilic domain II of the structural fimbrial subunit DraE and evaluated recombinant mutant DraE for attachment, invasion, and intracellular compartmentalization. The mutation of amino acids V28, T31, G33, Q34, T36, and P40 of DraE reduced or abolished HeLa cell invasion but did not affect attachment. Electron micrographs showed a stepwise entry and fusion of vacuoles containing Escherichia coli mutants T36A and Q34A or corresponding beads with lysosomes, whereas vacuoles with wild-type Dr adhesin showed no fusion. Mutants T31A and Q34A, which were deficient in invasion, appeared to display a reduced capacity for clustering decay-accelerating factor. Our findings suggest that hydrophilic domain II may be involved in cell entry. These data are consistent with the interpretation that in HeLa cells the binding and invasion phenotypes of Dr fimbriae may be separated.

* Corresponding author. Mailing address: Department of Obstetrics & Gynecology, University of Texas Medical Branch, 301 University Blvd., Galveston, TX 77555-1062. Phone: (409) 772-7599. Fax: (409) 747-0475. E-mail: bnowicki{at}utmb.edu.

Editor: V. J. DiRita

Infection and Immunity, September 2005, p. 6119-6126, Vol. 73, No. 9
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.9.6119-6126.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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