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Infection and Immunity, September 2001, p. 5914-5920, Vol. 69, No. 9
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.9.5914-5920.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Cloning, Expression, and Catalytic Activity of Helicobacter hepaticus Urease

Catherine S. Beckwith,1,* David J. McGee,2,dagger Harry L. T. Mobley,2 and Lela K. Riley1

Department of Veterinary Pathobiology, University of Missouri, Columbia, Missouri 65211,1 and Department of Microbiology and Immunology, University of Maryland, Baltimore, Maryland 212012

Received 2 February 2001/Returned for modification 18 April 2001/Accepted 15 June 2001

Helicobacter hepaticus causes disease in the liver and lower intestinal tract of mice. It is strongly urease positive, although it does not live in an acidic environment. The H. hepaticus urease gene cluster was expressed in Escherichia coli with and without coexpression of the Helicobacter pylori nickel transporter NixA. As for H. pylori, it was difficult to obtain enzymatic activity from recombinant H. hepaticus urease; special conditions including NiCl2 supplementation were required. The H. hepaticus urease cluster contains a homolog of each gene in the H. pylori urease cluster, including the urea transporter gene ureI. Downstream genes were homologs of the nik nickel transport operon of E. coli. Nongastric H. hepaticus produces urease similar to that of H. pylori.

* Corresponding author. Present address: Department of Comparative Medicine, Stanford University School of Medicine, Stanford, CA 94305-5410. Phone: (650) 723-5305. Fax: (650) 725-0940. E-mail: CBeckwith{at}Stanford.edu.

dagger Present address: Department of Microbiology and Immunology, College of Medicine, University of South Alabama, Mobile, AL 36688.

Infection and Immunity, September 2001, p. 5914-5920, Vol. 69, No. 9
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.9.5914-5920.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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