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Journal of Bacteriology, July 2001, p. 4099-4102, Vol. 183, No. 13
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.13.4099-4102.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Characterization of Escherichia coli Type 1 Pilus Mutants with Altered Binding Specificities

Sandra L. Harris, Patricia A. Spears, Edward A. Havell, Terri S. Hamrick, John R. Horton, and Paul E. Orndorff*

Department of Microbiology, Pathology, and Parasitology, College of Veterinary Medicine, North Carolina State University, Raleigh, North Carolina 27606

Received 19 January 2001/Accepted 13 April 2001

PCR mutagenesis and a unique enrichment scheme were used to obtain two mutants, each with a single lesion in fimH, the chromosomal gene that encodes the adhesin protein (FimH) of Escherichia coli type 1 pili. These mutants were noteworthy in part because both were altered in the normal range of cell types bound by FimH. One mutation altered an amino acid at a site previously shown to be involved in temperature-dependent binding, and the other altered an amino acid lining the predicted FimH binding pocket.

* Corresponding author. Mailing address: College of Veterinary Medicine, 4700 Hillsborough St., Raleigh, NC 27606. Phone: (919) 513-6207. Fax: (919) 513-6455. E-mail: Paul_Orndorff{at}ncsu.edu.

Journal of Bacteriology, July 2001, p. 4099-4102, Vol. 183, No. 13
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.13.4099-4102.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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