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Infection and Immunity, December 2001, p. 7941-7945, Vol. 69, No. 12
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.12.7941-7945.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Characterization of the Adhesin of Escherichia coli F18 Fimbriae

A. Smeds,1 K. Hemmann,1 M. Jakava-Viljanen,1 S. Pelkonen,2 H. Imberechts,3 and A. Palva1,*

Faculty of Veterinary Medicine, Department of Basic Veterinary Sciences, Section of Microbiology, 00014 University of Helsinki,1 and National and Veterinary Food Research Institute, Helsinki,2 Finland, and Laboratory of General Bacteriology, National Veterinary Research Institute, Brussels, Belgium3

Received 31 May 2001/Returned for modification 19 July 2001/Accepted 14 September 2001

Previous research has suggested that the adhesin encoded by the F18 fimbrial operon in Escherichia coli is either the FedE or FedF protein. In this work, we show that anti-FedF antibodies, unlike anti-FedE serum, were able to inhibit E. coli adhesion to porcine enterocytes. Moreover, specific adhesion to enterocytes was shown with purified FedF-maltose binding protein.

* Corresponding author. Mailing address: Faculty of Veterinary Medicine, Department of Basic Veterinary Sciences, Section of Microbiology P.O. Box 57, 00014 University of Helsinki, Finland. Phone: 358-9-19149531. Fax: 358-9-19149799. E-mail: airi.palva{at}helsinki.fi.

Infection and Immunity, December 2001, p. 7941-7945, Vol. 69, No. 12
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.12.7941-7945.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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