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 DeAngelis, P. L.
Right arrow Articles by White, C. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by DeAngelis, P. L.
Right arrow Articles by White, C. L.

 Previous Article  |  Next Article 

Journal of Bacteriology, December 2004, p. 8529-8532, Vol. 186, No. 24
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.24.8529-8532.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Identification of a Distinct, Cryptic Heparosan Synthase from Pasteurella multocida Types A, D, and F

Paul L. DeAngelis* and Carissa L. White

Department of Biochemistry and Molecular Biology, Oklahoma Center for Medical Glycobiology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma

Received 6 July 2004/ Accepted 18 August 2004

The extracellular polysaccharide capsules of Pasteurella multocida types A, D, and F are composed of hyaluronan, N-acetylheparosan (heparosan or unsulfated, unepimerized heparin), and unsulfated chondroitin, respectively. Previously, a type D heparosan synthase, a glycosyltransferase that forms the repeating disaccharide heparosan backbone, was identified. Here, a ~73% identical gene product that is encoded outside of the capsule biosynthesis locus was also shown to be a functional heparosan synthase. Unlike PmHS1, the PmHS2 enzyme was not stimulated greatly by the addition of an exogenous polymer acceptor and yielded smaller- molecular-weight-product size distributions. Virtually identical hssB genes are found in most type A, D, and F isolates. The occurrence of multiple polysaccharide synthases in a single strain invokes the potential for capsular variation.

* Corresponding author. Mailing address: Dept. of Biochemistry and Molecular Biology, Univ. of Oklahoma Health Sciences Center, 940 Stanton L. Young Blvd., Oklahoma City, OK 73104. Phone: (405) 271-2227. Fax: (405) 271-3092. E-mail: paul-deangelis{at}ouhsc.edu.

Journal of Bacteriology, December 2004, p. 8529-8532, Vol. 186, No. 24
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.24.8529-8532.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Tang, X., Zhao, Z., Hu, J., Wu, B., Cai, X., He, Q., Chen, H. (2009). Isolation, Antimicrobial Resistance, and Virulence Genes of Pasteurella multocida Strains from Swine in China. J. Clin. Microbiol. 47: 951-958 [Abstract] [Full Text]  
  • Sismey-Ragatz, A. E., Green, D. E., Otto, N. J., Rejzek, M., Field, R. A., DeAngelis, P. L. (2007). Chemoenzymatic Synthesis with Distinct Pasteurella Heparosan Synthases: MONODISPERSE POLYMERS AND UNNATURAL STRUCTURES. J. Biol. Chem. 282: 28321-28327 [Abstract] [Full Text]  
  • Tracy, B. S., Avci, F. Y., Linhardt, R. J., DeAngelis, P. L. (2007). Acceptor Specificity of the Pasteurella Hyaluronan and Chondroitin Synthases and Production of Chimeric Glycosaminoglycans. J. Biol. Chem. 282: 337-344 [Abstract] [Full Text]  
  • Kane, T. A., White, C. L., DeAngelis, P. L. (2006). Functional Characterization of PmHS1, a Pasteurella multocida Heparosan Synthase. J. Biol. Chem. 281: 33192-33197 [Abstract] [Full Text]  
  • Williams, K. J., Halkes, K. M., Kamerling, J. P., DeAngelis, P. L. (2006). Critical Elements of Oligosaccharide Acceptor Substrates for the Pasteurella multocida Hyaluronan Synthase. J. Biol. Chem. 281: 5391-5397 [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»