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
Right arrow Citation Map
Services
Right arrow E-mail this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ASM journals
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 Hissen, A. H. T.
Right arrow Articles by Moore, M. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hissen, A. H. T.
Right arrow Articles by Moore, M. M.

 Previous Article  |  Next Article 

Infection and Immunity, March 2004, p. 1402-1408, Vol. 72, No. 3
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.3.1402-1408.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Survival of Aspergillus fumigatus in Serum Involves Removal of Iron from Transferrin: the Role of Siderophores

A. H. T. Hissen, J. M. T. Chow, L. J. Pinto, and M. M. Moore*

Department of Biological Sciences, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada

Received 24 October 2003/ Returned for modification 1 December 2003/ Accepted 12 December 2003

Aspergillus fumigatus is a filamentous fungus which can cause invasive disease in immunocompromised individuals. A. fumigatus can grow in medium containing up to 80% human serum, despite very low concentrations of free iron. The purpose of this study was to determine the mechanism by which A. fumigatus obtains iron from the serum iron-binding protein transferrin. In iron-depleted minimal essential medium (MEM), A. fumigatus growth was supported by the addition of holotransferrin (holoTf) or FeCl3 but not by the addition of apotransferrin (apoTf). Proteolytic degradation of transferrin by A. fumigatus occurred in MEM-serum; however, transferrin degradation did not occur until late logarithmic phase. Moreover, transferrin was not degraded by A. fumigatus incubated in MEM-holoTf. Urea polyacrylamide gel electrophoresis showed that in MEM-holoTf, holoTf was completely converted to apoTf by A. fumigatus. In human serum, all of the monoferric transferrin was converted to apoTf within 8 h. Siderophores were secreted by A. fumigatus after 8 h of growth in MEM-serum and 12 h in MEM-holoTf. The involvement of small molecules in iron acquisition was confirmed by the fact that transferrin was deferrated by A. fumigatus even when physically separated by a 12-kDa-cutoff membrane. Five siderophores were purified from A. fumigatus culture medium, and the two major siderophores were identified as triacetylfusarinine C and ferricrocin. Both triacetylfusarinine C and ferricrocin removed iron from holoTf with an affinity comparable to that of ferrichrome. These data indicate that A. fumigatus survival in human serum in vitro involves siderophore-mediated removal of iron from transferrin. Proteolytic degradation of transferrin may play a secondary role in iron acquisition.

* Corresponding author. Mailing address: Department of Biological Sciences, Simon Fraser University, 8888 University Dr., Burnaby, British Columbia V5A 1S6, Canada. Phone: (604) 291-3441. Fax: (604) 291-3496. E-mail: mmoore{at}sfu.ca.

Editor: T. R. Kozel

Infection and Immunity, March 2004, p. 1402-1408, Vol. 72, No. 3
0019-9567/04/$08.00+0     DOI: 10.1128/IAI.72.3.1402-1408.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Jung, W. H., Hu, G., Kuo, W., Kronstad, J. W. (2009). Role of Ferroxidases in Iron Uptake and Virulence of Cryptococcus neoformans. Eukaryot Cell 8: 1511-1520 [Abstract] [Full Text]  
  • Zarember, K. A., Sugui, J. A., Chang, Y. C., Kwon-Chung, K. J., Gallin, J. I. (2007). Human Polymorphonuclear Leukocytes Inhibit Aspergillus fumigatus Conidial Growth by Lactoferrin-Mediated Iron Depletion. J. Immunol. 178: 6367-6373 [Abstract] [Full Text]  
  • Tangen, K. L., Jung, W. H., Sham, A. P., Lian, T., Kronstad, J. W. (2007). The iron- and cAMP-regulated gene SIT1 influences ferrioxamine B utilization, melanization and cell wall structure in Cryptococcus neoformans. Microbiology 153: 29-41 [Abstract] [Full Text]  
  • Knight, S. A. B., Vilaire, G., Lesuisse, E., Dancis, A. (2005). Iron Acquisition from Transferrin by Candida albicans Depends on the Reductive Pathway. Infect. Immun. 73: 5482-5492 [Abstract] [Full Text]  
  • Hissen, A. H. T., Wan, A. N. C., Warwas, M. L., Pinto, L. J., Moore, M. M. (2005). The Aspergillus fumigatus Siderophore Biosynthetic Gene sidA, Encoding L-Ornithine N5-Oxygenase, Is Required for Virulence. Infect. Immun. 73: 5493-5503 [Abstract] [Full Text]  
  • Vicentefranqueira, R., Moreno, M. A., Leal, F., Calera, J. A. (2005). The zrfA and zrfB Genes of Aspergillus fumigatus Encode the Zinc Transporter Proteins of a Zinc Uptake System Induced in an Acid, Zinc-Depleted Environment. Eukaryot Cell 4: 837-848 [Abstract] [Full Text]  
  • Schrettl, M., Bignell, E., Kragl, C., Joechl, C., Rogers, T., Arst, H. N. Jr., Haynes, K., Haas, H. (2004). Siderophore Biosynthesis But Not Reductive Iron Assimilation Is Essential for Aspergillus fumigatus Virulence. JEM 200: 1213-1219 [Abstract] [Full Text]  
  • Missall, T. A., Lodge, J. K., McEwen, J. E. (2004). Mechanisms of Resistance to Oxidative and Nitrosative Stress: Implications for Fungal Survival in Mammalian Hosts. Eukaryot Cell 3: 835-846 [Full Text]  


Copyright © 2010 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»