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Bacillus anthracis IsdG, a Heme-Degrading Monooxygenase
Open accessAbstract
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.
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“The Bacillus anthracis Isd proteins include IsdX1 and IsdX2, which are secreted haemophores that bind haemoglobin, haptoglobin-haemoglobin or haem 33-35 .”
From Nutritional immunity: the battle for nutrient metals at the host–pathogen interface (2022) · cites this paper as [35]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“The disruption of B. anthracis isdG causes growth inhibition across all concentrations of heme, when heme is the sole iron source (101).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [101]
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In the citing paper
“This suggests that IsdG is needed both for the utilization of iron from heme and for the prevention of heme toxicity.”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [101]
In the citing paper
“IsdDEF transports heme across the membrane for utilization by IsdG, an orthologue of the S. aureus heme oxygenase [133].”
From Heme Synthesis and Acquisition in Bacterial Pathogens (2016) · cites this paper as [133]
In the citing paper
“IsdG-family heme oxygenases have been characterized in S. lugdunensis, Bacillus anthracis, Bradyrhizobium japonicum, Brucella melitensis, and Mycobacterium tuberculosis [46, 50, 56–58].”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [58]
In the citing paper
“While IsdG orthologs from each of these bacteria have been shown to bind and degrade heme, differences do exist.”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [58]
In the citing paper
“IsdG family heme oxygenases have been characterized for S. aureus , B. anthracis , B. japonicum , Mycobacterium tuberculosis , and Brucella melitensis and are predicted to be encoded in the Alphaproteobacteria , Streptomyces , Deinococcus-Thermus , and Chloroflexi groups (17, 89, 101, 102).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [101]
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Cites
Basic local alignment search tool
Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669
Dixon, T. C., Meselson, M. S., Guillemin, J. H., & Hanna, P. C. (1999) · New England Journal of Medicine · doi:10.1056/nejm199909093411107 · Cited by 871
The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria
Read, T. D., Peterson, S. N., Tourasse, N. J., Baillie, L. W. J., Paulsen, I. T., Nelson, K. E., Tettelin, H., Fouts, D. E., Eisen, J. A., Gill, S. R., et al. (2003) · Nature · doi:10.1038/nature01586 · Cited by 822
Opening the Iron Box: Transcriptional Metalloregulation by the Fur Protein
Escolar, L., Pérez-Martín, J., & de Lorenzo, V. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.20.6223-6229.1999 · Cited by 815
The significance of iron in infection
Bullen, J. J. (1981) · Clinical Infectious Diseases · doi:10.1093/clinids/3.6.1127 · Cited by 603
Passage of Heme-Iron Across the Envelope of Staphylococcus aureus
Mazmanian, S. K., Skaar, E. P., Gaspar, A. H., Humayun, M., Gornicki, P., Jelenska, J., Joachmiak, A., Missiakas, D. M., & Schneewind, O. (2003) · Science · doi:10.1126/science.1081147 · Cited by 593
Self-citationCollier, R. J., & Young, J. A. T. (2003) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.19.111301.140655 · Cited by 510
Demonstration of a capsule plasmid in Bacillus anthracis
Green, B. D., Battisti, L., Koehler, T. M., Thorne, C. B., & Ivins, B. E. (1985) · Infection and Immunity · doi:10.1128/iai.49.2.291-297.1985 · Cited by 491
Iron-Source Preference of Staphylococcus aureus Infections
Skaar, E. P., Humayun, M., Bae, T., DeBord, K. L., & Schneewind, O. (2004) · Science · doi:10.1126/science.1099930 · Cited by 440
Self-citationMazmanian, S. K., Ton-That, H., Su, K., & Schneewind, O. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.032523999 · Cited by 372
Self-citation
Research works printed but not linked: 2
- 10.1016/S0022-2836(05)80360-2 · DOI · Paper page
- Sambrook J. E. F. Fritsch and T. Maniatis. 1989. Molecular cloning: a laboratory manual 2nd ed. Cold Spring Harbor Press Cold Spring Harbor N.Y.
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Metadata
- Authors
- Skaar, E. P., Gaspar, A. H., & Schneewind, O.
- Affiliations
- University of Chicago (US)
- Corresponding author
- Schneewind, Olaf
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 2006-02
- Volume
- 188
- Issue
- 3
- Pages
- 1071-1080
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- PMC
- PMC1347327
- OpenAlex
- W2140572324
- Cited by
- 123
- References
- 61
- Citations by year
- 2026: 4 · 2025: 5 · 2023: 4 · 2022: 3 · 2020: 6 · 2019: 4 · 2018: 7 · 2017: 5 · 2016: 8 · 2015: 1 · 2014: 1 · 2013: 9 · 2012: 11
- FWCI
- 5.02
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Bacteriology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Heart Association
- Great Lakes Regional Center of Excellence for Biodefense and Emerging Infectious Diseases Research (057153)
- U.S. Public Health Service
- National Institute of Allergy and Infectious Diseases (U54AI057153, AI38897, AI52474, R01AI038897, R01AI052474)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bacillus and Francisella bacterial research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- Bacillus anthracis, heme oxygenase, iron acquisition, heme binding, biliverdin, hemoglobin, anthrax
- MeSH terms
- Amino Acid Sequence, Bacillus anthracis, Heme, Heme Oxygenase (Decyclizing), Iron, Molecular Sequence Data, Oxygenases
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