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 Howard, D. H.
Right arrow Articles by Faull, K. F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Howard, D. H.
Right arrow Articles by Faull, K. F.

 Previous Article  |  Next Article 

Infection and Immunity, April 2000, p. 2338-2343, Vol. 68, No. 4
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Hydroxamate Siderophores of Histoplasma capsulatum

Dexter H. Howard,1,* Ramin Rafie,1 Anupama Tiwari,1 and Kym F. Faull2

Department of Microbiology and Immunology,1 and The Pasarow Mass Spectroscopy Laboratory, Departments of Chemistry and Biochemistry, Psychiatry and Biobehavioral Sciences, and the Neuropsychiatric Institute,2 UCLA School of Medicine, Los Angeles, California

Received 31 August 1999/Returned for modification 30 September 1999/Accepted 3 January 2000

The zoopathogenic fungus Histoplasma capsulatum, like other eukaryotic aerobic microorganisms, requires iron for growth. Under conditions of low iron availability, the fungus secretes hydroxamates that function as siderophores (iron chelators). The experiments to be reported were designed to gather further information on the hydroxamate siderophores of H. capsulatum. The fungus was grown in a synthetic medium deferrated with the cationic exchange resin Chelex 100. Siderophores were detected after 4 days of incubation at 37°C in media containing 0.3 to 1.0 µM iron. The secretion was suppressed by 10 µM iron. The hydroxamates were purified by reverse-phase and size-exclusion chromatography. On the basis of ions observed during electrospray mass spectroscopy, five hydroxamate siderophores were tentatively identified: dimerum acid, acetyl dimerum acid, coprogen B, methyl coprogen B, and fusarinine (monomeric). A polyclonal antibody to dimerum acid was generated. This reagent cross-reacted with coprogen B and fusarinine. Thus, the antibody detects hydroxamates in all three families of siderophores excreted by H. capsulatum.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, UCLA School of Medicine, Los Angeles, CA 90095-1747. Phone: (310) 825-6661. Fax: (310) 206-3865. E-mail: dhoward{at}ucla.edu.

Infection and Immunity, April 2000, p. 2338-2343, Vol. 68, No. 4
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Zarnowski, R., Woods, J. P. (2005). Glutathione-dependent extracellular ferric reductase activities in dimorphic zoopathogenic fungi. Microbiology 151: 2233-2240 [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]  
  • Hissen, A. H. T., Chow, J. M. T., Pinto, L. J., Moore, M. M. (2004). Survival of Aspergillus fumigatus in Serum Involves Removal of Iron from Transferrin: the Role of Siderophores. Infect. Immun. 72: 1402-1408 [Abstract] [Full Text]  
  • Timmerman, M. M., Woods, J. P. (2001). Potential Role for Extracellular Glutathione-Dependent Ferric Reductase in Utilization of Environmental and Host Ferric Compounds by Histoplasma capsulatum. Infect. Immun. 69: 7671-7678 [Abstract] [Full Text]  
  • Wilhite, S. E., Lumsden, R. D., Straney, D. C. (2001). Peptide Synthetase Gene in Trichoderma virens. Appl. Environ. Microbiol. 67: 5055-5062 [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»