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Infection and Immunity, June 2003, p. 3068-3075, Vol. 71, No. 6
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.6.3068-3075.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Role of Phosphoglucomutase of Stenotrophomonas maltophilia in Lipopolysaccharide Biosynthesis, Virulence, and Antibiotic Resistance

Department of Microbiology and Immunology, Queen's University, Kingston, Ontario, Canada K7L 3N6,¹ Department of Microbiology and Infectious Diseases, Faculty of Medicine, University of Calgary Health Sciences Centre, Calgary, Alberta, Canada T2N 4N1,² British Columbia Research Centre for Children and Women's Health, Vancouver, British Columbia, Canada V5Z 4H4³

Received 18 November 2002/ Returned for modification 14 February 2003/ Accepted 28 February 2003

A homologue of the algC gene, responsible for the production of a phosphoglucomutase (PGM) associated with LPS and alginate biosynthesis in Pseudomonas aeruginosa, spgM, was cloned from Stenotrophomonas maltophilia. The spgM gene was shown to encode a bifunctional enzyme with both PGM and phosphomannomutase activities. Mutants lacking spgM produced less LPS than the SpgM⁺ parent strain and had a tendency for shorter O polysaccharide chains. No changes in LPS chemistry were obvious as a result of the loss of spgM. Significantly, however, spgM mutants displayed a modest increase in susceptibility to several antimicrobial agents and were completely avirulent in an animal model of infection. The latter finding may relate to the resultant serum sensitivity of spgM mutants which, unlike the wild-type parent strain, were rapidly killed by human serum. These data highlight the contribution made by LPS to the antimicrobial resistance and virulence of S. maltophilia.

Editor: J. D. Clements

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