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Applied and Environmental Microbiology, January 2000, p. 10-14, Vol. 66, No. 1
0099-2240/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Sequestration of Zinc Oxide by Fimbrial Designer Chelators

Kristian Kjærgaard, Jack K. Sørensen, Mark A. Schembri, and Per Klemm*

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

Received 2 August 1999/Accepted 10 October 1999

Type 1 fimbriae are surface organelles of Escherichia coli. By engineering a structural component of the fimbriae, FimH, to display a random peptide library, we were able to isolate metal-chelating bacteria. A library consisting of 4 × 107 independent clones was screened for binding to ZnO. Sequences responsible for ZnO adherence were identified, and distinct binding motifs were characterized. The sequences selected exhibited various degrees of affinity and specificity towards ZnO. Competitive binding experiments revealed that the sequences recognized only the oxide form of Zn. Interestingly, one of the inserts exhibited significant homology to a specific sequence in a putative zinc-containing helicase, which suggests that searches such as this one may aid in identifying binding motifs in nature. The zinc-binding bacteria might have a use in detoxification of metal-polluted water.

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

Applied and Environmental Microbiology, January 2000, p. 10-14, Vol. 66, No. 1
0099-2240/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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