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Appl Environ Microbiol, May 1998, p. 1628-1633, Vol. 64, No. 5
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Heterobinary Adhesins Based on the Escherichia coli FimH Fimbrial Protein

Mark A. Schembri and Per Klemm*

Department of Microbiology, Technical University of Denmark, DK-2800 Lyngby, Denmark

Received 1 December 1997/Accepted 16 February 1998

The FimH adhesin of Escherichia coli type 1 fimbriae confers the ability to bind to D-mannosides by virtue of a receptor-binding domain located in its N-terminal region. This protein was engineered into a heterobifunctional adhesin by introducing a secondary binding site in the C-terminal region. The insertion of histidine clusters into this site resulted in coordination of various metal ions by recombinant cells expressing chimeric FimH proteins. In addition, libraries consisting of random peptide sequences inserted into the FimH display system and screened by a "panning" technique were used to identify specific sequences conferring the ability to adhere to Ni2+ and Cu2+. Recombinant cells expressing heterobifunctional FimH adhesins could adhere simultaneously to both metals and saccharides. Finally, combining the metal-binding modifications with alterations in the natural receptor-binding region demonstrated the ability to independently modulate the binding of FimH to two ligands simultaneously.

* Corresponding author. Mailing address: Department of Microbiology, Building 301, Technical University of Denmark, DK-2800 Lyngby, Denmark. Phone: 45 45 25 25 06. Fax: 45 45 93 28 09. E-mail: pk{at}im.dtu.dk.

Appl Environ Microbiol, May 1998, p. 1628-1633, Vol. 64, No. 5
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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