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Infection and Immunity, August 2000, p. 4673-4680, Vol. 68, No. 8
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Role of Phosphoglucomutase of Bordetella bronchiseptica in Lipopolysaccharide Biosynthesis and Virulence

Nicholas P. West,1 Heidrun Jungnitz,2 John T. Fitter,1,dagger Jason D. McArthur,1 Carlos A. Guzmán,2 and Mark J. Walker1,*

Department of Biological Sciences, University of Wollongong, New South Wales, Australia,1 and Department of Microbial Pathogenicity and Vaccine Research, Division of Microbiology, GBF-National Research Centre for Biotechnology, Braunschweig, Germany2

Received 8 November 1999/Returned for modification 3 January 2000/Accepted 5 May 2000

The phosphoglucomutase (PGM)-encoding gene of Bordetella bronchiseptica is required for lipopolysaccharide (LPS) biosynthesis. An insertion mutant of the wild-type B. bronchiseptica strain BB7865 which disrupted LPS biosynthesis was created and characterized (BB7865pgm). Genetic analysis of the mutated gene showed it shares high identity with PGM genes of various bacterial species and forms part of an operon which also encompasses the gene encoding phosphoglucose isomerase. Functional assays for PGM revealed that enzyme activity is expressed in both bvg-positive and bvg-negative strains of B. bronchiseptica and is substantially reduced in BB7865pgm. Complementation of the mutated PGM gene with that from BB7865 restored the wild-type condition for all phenotypes tested. The ability of the mutant BB7865pgm to survive within J774.A1 cells was significantly reduced at 2 h (40% reduction) and 24 h (56% reduction) postinfection. BB7865pgm was also significantly attenuated in its ability to survive in vivo following intranasal infection of mice, being effectively cleared from the lungs within 4 days, whereas the wild-type strain persisted at least 35 days. The activities of superoxide dismutase, urease, and acid phosphatase were unaffected in the PGM-deficient strain. In contrast, the inability to produce wild-type LPS resulted in a reduced bacterial resistance to oxidative stress and a higher susceptibility to the antimicrobial peptide cecropin P.

* Corresponding author. Mailing address: Department of Biological Sciences, University of Wollongong, New South Wales, Australia 2522. Phone: 0061-242213439. Fax: 0061-242214135. E-mail: mwalker{at}uow.edu.au.

dagger Present address: Endocrine Unit, Department of Medicine, John Hunter Hospital, Newcastle, New South Wales, Australia.

Infection and Immunity, August 2000, p. 4673-4680, Vol. 68, No. 8
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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