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 Ogunnariwo, J. A.
Right arrow Articles by Schryvers, A. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ogunnariwo, J. A.
Right arrow Articles by Schryvers, A. B.

 Previous Article  |  Next Article 

Journal of Bacteriology, February 2001, p. 890-896, Vol. 183, No. 3
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.3.890-896.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Characterization of a Novel Transferrin Receptor in Bovine Strains of Pasteurella multocida

Julius A. Ogunnariwo and Anthony B. Schryvers*

Department of Microbiology and Infectious Diseases, University of Calgary, Calgary, Alberta, Canada T2N 4N1

Received 15 September 2000/Accepted 10 November 2000

Analysis of bovine respiratory isolates of Pasteurella multocida demonstrated that six of nine strains tested were capable of growth dependent upon bovine transferrin and of specifically binding ruminant transferrins. A single 82-kDa protein was affinity isolated from the P. multocida strains with immobilized bovine transferrin. In contrast to what has been observed in other species, binding of this protein to immobilized transferrin was specifically blocked by the N-lobe subfragment of bovine transferrin. A single gene encoding the 82-kDa protein was flanked by a leucyl-tRNA synthetase gene and an IS1060 element, in contrast to other species where genes encoding the two receptor proteins (TbpB and TbpA) are found in an operonic arrangement. A similar gene arrangement was observed in all of the receptor-positive strains, in spite of the observation that they belonged to different genomic groups. Analysis of the deduced amino acid sequence of the receptor protein indicated that it is a member of the TonB-dependent outer membrane receptor family, and although it is related to transferrin and lactoferrin receptor proteins (TbpAs and LbpAs) from other species, it differs substantially from other members of this group. Amino acid alignments suggest that the reduced size (20 kDa smaller) of the P. multocida TbpA is primarily due to the absence of larger predicted external loops. Collectively these results suggest that P. multocida has a single, novel receptor protein (TbpA) that is capable of efficiently mediating iron acquisition from bovine transferrin without the involvement of a second receptor protein (TbpB).

* Corresponding author. Mailing address: Rm. 274, Heritage Medical Research Building, 3330 Hospital Dr. N.W., Calgary, Alberta, Canada T2N 4N. Phone: (403) 220-3703. Fax: (403) 270-2772. E-mail: schryver{at}ucalgary.ca.

Journal of Bacteriology, February 2001, p. 890-896, Vol. 183, No. 3
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.3.890-896.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Wheeler, R. (2009). Outer membrane proteomics of Pasteurella multocida isolates to identify putative host-specificity determinants. Bioscience Horizons 2: 1-12 [Abstract] [Full Text]  
  • Ekins, A., Bahrami, F., Sijercic, A., Maret, D., Niven, D. F. (2004). Haemophilus somnus Possesses Two Systems for Acquisition of Transferrin-Bound Iron. J. Bacteriol. 186: 4407-4411 [Abstract] [Full Text]  
  • Renauld-Mongenie, G., Poncet, D., Mignon, M., Fraysse, S., Chabanel, C., Danve, B., Krell, T., Quentin-Millet, M.-J. (2004). Role of Transferrin Receptor from a Neisseria meningitidis tbpB Isotype II Strain in Human Transferrin Binding and Virulence. Infect. Immun. 72: 3461-3470 [Abstract] [Full Text]  
  • Perkins-Balding, D., Ratliff-Griffin, M., Stojiljkovic, I. (2004). Iron Transport Systems in Neisseria meningitidis. Microbiol. Mol. Biol. Rev. 68: 154-171 [Abstract] [Full Text]  
  • Sims, K. L., Schryvers, A. B. (2003). Peptide-Peptide Interactions between Human Transferrin and Transferrin-Binding Protein B from Moraxellacatarrhalis. J. Bacteriol. 185: 2603-2610 [Abstract] [Full Text]  
  • Ekins, A., Niven, D. F. (2002). Identification of fur and fldA Homologs and a Pasteurella multocida tbpA Homolog in Histophilus ovis and Effects of Iron Availability on Their Transcription. J. Bacteriol. 184: 2539-2542 [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»