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A Heptosyltransferase Mutant of Pasteurella multocida Produces a Truncated Lipopolysaccharide Structure and Is Attenuated in Virulence

Australian Bacterial Pathogenesis Program, Department of Microbiology,¹ Australian Research Council Centre for Structural and Functional Microbial Genomics, Monash University, Melbourne, Victoria 3800,² Veterinary Pathology and Anatomy, University of Queensland, Brisbane, Queensland 4072, Australia,⁴ Institute for Biological Sciences, National Research Council, Ottawa, Canada³

Received 11 November 2003/ Returned for modification 10 February 2004/ Accepted 27 February 2004

Pasteurella multocida is the causative agent of fowl cholera in birds. In a previous study using signature-tagged mutagenesis, we identified a mutant, AL251, which was attenuated for virulence in mice and in the natural chicken host. Sequence analysis indicated that AL251 had an insertional inactivation of the gene waaQ_PM, encoding a putative heptosyl transferase, required for the addition of heptose to lipopolysaccharide (LPS) (M. Harper, J. D. Boyce, I. W. Wilkie, and B. Adler, Infect. Immun. 71:5440-5446, 2003). In the present study, using mass spectrometry and nuclear magnetic resonance, we have confirmed the identity of the enzyme encoded by waaQ_PM as a heptosyl transferase III and demonstrated that the predominant LPS glycoforms isolated from this mutant are severely truncated. Complementation experiments demonstrated that providing a functional waaQ_PM gene in trans can restore both the LPS to its full length and growth in mice to wild-type levels. Furthermore, we have shown that mutant AL251 is unable to cause fowl cholera in chickens and that the attenuation observed is not due to increased serum sensitivity.

Editor: V. J. DiRita

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