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Journal of Bacteriology, February 2006, p. 1071-1080, Vol. 188, No. 3
0021-9193/06/$08.00+0 doi:10.1128/JB.188.3.1071-1080.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Andrew H. Gaspar,
and
Olaf Schneewind*
Department of Microbiology, University of Chicago, Chicago, Illinois 60637
Received 2 August 2005/ Accepted 9 November 2005
Bacillus anthracis, the causative agent of anthrax, utilizes hemin and hemoglobin for growth in culture, suggesting that these host molecules serve as sources for the nutrient iron during bacterial infection. Bioinformatic analyses of the B. anthracis genome revealed genes with similarity to the iron-regulated surface determinant (isd) system responsible for heme uptake in Staphylococcus aureus. We show that the protein product of one of these genes, isdG, binds hemin in a manner resembling the heme binding of known heme oxygenases. Formation of IsdG:hemin complexes in the presence of a suitable electron donor, e.g., ascorbate or cytochrome P450 reductase, promotes catalytic degradation of hemin to biliverdin with concomitant release of iron. IsdG is required for B. anthracis utilization of hemin as a sole iron source, and it is also necessary for bacterial protection against heme-mediated toxicity. These data suggest that IsdG functions as a heme-degrading monooxygenase in B. anthracis.
Present address: Department of Microbiology and Immunology, Vanderbilt University Medical Center, 1161 21st Avenue South, Nashville, TN 37232.
Present address: Department of Molecular, Microbial, and Structural Biology, University of Connecticut Health Center, 263 Farmington Ave., Farmington, CT 06030.
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