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Infection and Immunity, April 2009, p. 1532-1542, Vol. 77, No. 4
0019-9567/09/$08.00+0     doi:10.1128/IAI.01144-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Identification of Novel Glycosyltransferases Required for Assembly of the Pasteurella multocida A:1 Lipopolysaccharide and Their Involvement in Virulence{triangledown} ,{dagger}

John D. Boyce,1,2,{ddagger} Marina Harper,1,{ddagger} Frank St. Michael,3 Marietta John,1 Annie Aubry,3 Henrietta Parnas,3 Susan M. Logan,3 Ian W. Wilkie,4 Mark Ford,5 Andrew D. Cox,3 and Ben Adler1,2*

Australian Research Council Centre of Excellence in Structural and Functional Microbial Genomics, Monash University, Victoria 3800, Australia,1 Victorian Bioinformatics Consortium, Monash University, Victoria 3800, Australia,2 Institute for Biological Sciences, National Research Council, Ottawa, K1A0R6, Canada,3 Veterinary Pathology and Anatomy, University of Queensland, St Lucia, Queensland 4072, Australia,4 CSIRO Livestock Industries, Australian Animal Health Laboratory, Geelong, Victoria 3220, Australia5

Received 15 September 2008/ Returned for modification 17 October 2008/ Accepted 10 January 2009

We previously determined the structure of the Pasteurella multocida Heddleston type 1 lipopolysaccharide (LPS) molecule and characterized some of the transferases essential for LPS biosynthesis. We also showed that P. multocida strains expressing truncated LPS display reduced virulence. Here, we have identified all of the remaining glycosyltransferases required for synthesis of the oligosaccharide extension of the P. multocida Heddleston type 1 LPS, including a novel {alpha}-1,6 glucosyltransferase, a β-1,4 glucosyltransferase, a putative bifunctional galactosyltransferase, and two heptosyltransferases. In addition, we identified a novel oligosaccharide extension expressed only in a heptosyltransferase (hptE) mutant background. All of the analyzed mutants expressing LPS with a truncated main oligosaccharide extension displayed reduced virulence, but those expressing LPS with an intact heptose side chain were able to persist for long periods in muscle tissue. The hptC mutant, which expressed LPS with the shortest oligosaccharide extension and no heptose side chain, was unable to persist on the muscle or cause any disease. Furthermore, all of the mutants displayed increased sensitivity to the chicken antimicrobial peptide fowlicidin 1, with mutants expressing highly truncated LPS being the most sensitive.

* Corresponding author. Mailing address: Australian Research Council Centre of Excellence in Structural and Functional Microbial Genomics, Monash University, VIC 3800, Australia. Phone: 61 3 9905-4815. Fax: 61 3 9905-4811. E-mail: Ben.Adler{at}med.monash.edu.au

{triangledown} Published ahead of print on 21 January 2009.

{dagger} Supplemental material for this article may be found at http://iai.asm.org/.

Editor: F. C. Fang

{ddagger} J.D.B. and M.H. contributed equally to the work.

Infection and Immunity, April 2009, p. 1532-1542, Vol. 77, No. 4
0019-9567/09/$08.00+0     doi:10.1128/IAI.01144-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • St. Michael, F., Harper, M., Parnas, H., John, M., Stupak, J., Vinogradov, E., Adler, B., Boyce, J. D., Cox, A. D. (2009). Structural and Genetic Basis for the Serological Differentiation of Pasteurella multocida Heddleston Serotypes 2 and 5. J. Bacteriol. 191: 6950-6959 [Abstract] [Full Text]  


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