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 Miller, C. E.
Right arrow Articles by Ketley, J. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Miller, C. E.
Right arrow Articles by Ketley, J. M.

 Previous Article  |  Next Article 

Journal of Bacteriology, March 2008, p. 1900-1911, Vol. 190, No. 6
0021-9193/08/$08.00+0     doi:10.1128/JB.01761-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Utilization of Lactoferrin-Bound and Transferrin-Bound Iron by Campylobacter jejuni{triangledown}

Claire E. Miller, Jonathan D. Rock, Kristian A. Ridley, Peter H. Williams, and Julian M. Ketley*

Department of Genetics, University of Leicester, Leicester LE1 7RH, United Kingdom

Received 5 November 2007/ Accepted 3 January 2008

Campylobacter jejuni NCTC 11168 was capable of growth to levels comparable with FeSO4 in defined iron-limited medium (minimal essential medium alpha [MEM{alpha}]) containing ferrilactoferrin, ferritransferrin, or ferri-ovotransferrin. Iron was internalized in a contact-dependent manner, with 94% of cell-associated radioactivity from either 55Fe-loaded transferrin or lactoferrin associated with the soluble cell fraction. Partitioning the iron source away from bacteria significantly decreased cellular growth. Excess cold transferrin or lactoferrin in cultures containing 55Fe-loaded transferrin or lactoferrin resulted in reduced levels of 55Fe uptake. Growth of C. jejuni in the presence of ferri- and an excess of apoprotein reduced overall levels of growth. Following incubation of cells in the presence of ferrilactoferrin, lactoferrin became associated with the cell surface; binding levels were higher after growth under iron limitation. A strain carrying a mutation in the cj0178 gene from the iron uptake system Cj0173c-Cj0178 demonstrated significantly reduced growth promotion in the presence of ferrilactoferrin in MEM{alpha} compared to wild type but was not affected in the presence of heme. Moreover, this mutant acquired less 55Fe than wild type when incubated with 55Fe-loaded protein and bound less lactoferrin. Complementation restored the wild-type phenotype when cells were grown with ferrilactoferrin. A mutant in the ABC transporter system permease gene (cj0174c) showed a small but significant growth reduction. The cj0176c-cj0177 intergenic region contains two separate Fur-regulated iron-repressible promoters. This is the first demonstration that C. jejuni is capable of acquiring iron from members of the transferrin protein family, and our data indicate a role for Cj0178 in this process.


* Corresponding author. Mailing address: Department of Genetics, Adrian Building, University Road, University of Leicester, Leicester LE1 7RH, United Kingdom. Phone: 44 1162523434. Fax: 44 1162523378. E-mail: ket{at}leicester.ac.uk

{triangledown} Published ahead of print on 18 January 2008.


Journal of Bacteriology, March 2008, p. 1900-1911, Vol. 190, No. 6
0021-9193/08/$08.00+0     doi:10.1128/JB.01761-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Miller, C. E., Williams, P. H., Ketley, J. M. (2009). Pumping iron: mechanisms for iron uptake by Campylobacter. Microbiology 155: 3157-3165 [Abstract] [Full Text]  
  • Carswell, C. L., Rigden, M. D., Baenziger, J. E. (2008). Expression, Purification, and Structural Characterization of CfrA, a Putative Iron Transporter from Campylobacter jejuni. J. Bacteriol. 190: 5650-5662 [Abstract] [Full Text]