This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Steenbergen, S. M.
Right arrow Articles by Vimr, E. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Steenbergen, S. M.
Right arrow Articles by Vimr, E. R.

 Previous Article  |  Next Article 

Infection and Immunity, March 2005, p. 1284-1294, Vol. 73, No. 3
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.3.1284-1294.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Sialic Acid Metabolism and Systemic Pasteurellosis

Susan M. Steenbergen,1 Carol A. Lichtensteiger,1 Ruth Caughlan,1,{dagger} Jackie Garfinkle,1,{ddagger} Troy E. Fuller,2 and Eric R. Vimr1*

Laboratory of Sialobiology, Department of Pathobiology, University of Illinois at Urbana-Champaign, Urbana, Illinois,1 Pfizer Animal Health, Kalamazoo, Michigan2

Received 24 June 2004/ Returned for modification 13 August 2004/ Accepted 27 October 2004

Pasteurella multocida subsp. multocida is a commensal and opportunistic pathogen of food animals, wildlife, and pets and a zoonotic cause of human infection arising from contacts with these animals. Here, an investigation of multiple serotype A strains demonstrated the occurrence of membrane sialyltransferase. Although P. multocida lacks the genes for the two earliest steps in de novo sialic acid synthesis, adding sialic acid to the growth medium resulted in uptake, activation, and subsequent transfer of sialic acid to a membrane acceptor resembling lipooligosaccharide. Two candidate-activating enzymes with homology to Escherichia coli cytidine 5'-monophospho-N-acetylneuraminate synthetase were overproduced as histidine-tagged polypeptides. The synthetase encoded by pm0187 was at least 37 times more active than the pm1710 gene product, suggesting pm0187 encodes the primary sialic acid cytidylyltransferase in P. multocida. A sialate aldolase (pm1715) mutant unable to initiate dissimilation of internalized sialic acid was not attenuated in the CD-1 mouse model of systemic pasteurellosis, indicating that the nutritional function of sialate catabolism is not required for systemic disease. In contrast, the attenuation of a sialate uptake-deficient mutant supports the essential role in pathogenesis of a sialylation mechanism that is dependent on an environmental (host) supply of sialic acid. The combined results provide the first direct evidence of sialylation by a precursor scavenging mechanism in pasteurellae and of a potential tripartite ATP-independent periplasmic sialate transporter in any species.

* Corresponding author. Mailing address: 2522 VMBSB, 2001 South Lincoln Ave., Urbana, IL 61802. Phone: (217) 333-8502. Fax: (217) 244-7421. E-mail: ervimr{at}uiuc.edu.

Editor: J. T. Barbieri

{dagger} Present address: Department of Molecular Biology and Microbiology, Tufts University, Boston, MA 02115.

{ddagger} Present address: DNA Indexing Laboratory, Springfield, IL 62707.

Infection and Immunity, March 2005, p. 1284-1294, Vol. 73, No. 3
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.3.1284-1294.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Steenbergen, S. M., Jirik, J. L., Vimr, E. R. (2009). YjhS (NanS) Is Required for Escherichia coli To Grow on 9-O-Acetylated N-Acetylneuraminic Acid. J. Bacteriol. 191: 7134-7139 [Abstract] [Full Text]  
  • Almagro-Moreno, S., Boyd, E. F. (2009). Sialic Acid Catabolism Confers a Competitive Advantage to Pathogenic Vibrio cholerae in the Mouse Intestine. Infect. Immun. 77: 3807-3816 [Abstract] [Full Text]  
  • Thompson, H., Homer, K. A., Rao, S., Booth, V., Hosie, A. H. F. (2009). An Orthologue of Bacteroides fragilis NanH Is the Principal Sialidase in Tannerella forsythia. J. Bacteriol. 191: 3623-3628 [Abstract] [Full Text]  
  • Severi, E., Hood, D. W., Thomas, G. H. (2007). Sialic acid utilization by bacterial pathogens. Microbiology 153: 2817-2822 [Abstract] [Full Text]  
  • Steenbergen, S. M., Lee, Y.-C., Vann, W. F., Vionnet, J., Wright, L. F., Vimr, E. R. (2006). Separate Pathways for O Acetylation of Polymeric and Monomeric Sialic Acids and Identification of Sialyl O-Acetyl Esterase in Escherichia coli K1.. J. Bacteriol. 188: 6195-6206 [Abstract] [Full Text]  
  • Muller, A., Severi, E., Mulligan, C., Watts, A. G., Kelly, D. J., Wilson, K. S., Wilkinson, A. J., Thomas, G. H. (2006). Conservation of Structure and Mechanism in Primary and Secondary Transporters Exemplified by SiaP, a Sialic Acid Binding Virulence Factor from Haemophilus influenzae. J. Biol. Chem. 281: 22212-22222 [Abstract] [Full Text]  
  • Post, D. M. B., Mungur, R., Gibson, B. W., Munson, R. S. Jr. (2005). Identification of a Novel Sialic Acid Transporter in Haemophilus ducreyi. Infect. Immun. 73: 6727-6735 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»