Bacillus anthracis IsdG, a Heme-Degrading Monooxygenase

Skaar, Eric P.; Gaspar, Andrew H.; Schneewind, Olaf

doi:10.1128/jb.188.3.1071-1080.2006

Cited by 123Bacillus and Francisella bacterial researchHemoglobin structure and functionBacterial Genetics and Biotechnology

Bacillus anthracis IsdG, a Heme-Degrading Monooxygenase

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Skaar, Eric P., Gaspar, Andrew H., Schneewind, Olaf·2006·Journal of Bacteriology

DOI 10.1128/jb.188.3.1071-1080.2006PMC PMC1347327

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Abstract

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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Bacillus anthracis Isd proteins include IsdX1 and IsdX2, which are secreted haemophores that bind haemoglobin, haptoglobin-haemoglobin or haem.
“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]
The Results identify an isdX gene in the B. anthracis Isd cluster, and the introductory passage says B. anthracis uses hemin and hemoglobin for growth. Neither passage identifies IsdX1 and IsdX2 or says they are secreted haemophores that bind hemoglobin, haptoglobin–hemoglobin, or haem. (LLM, conf=0.77)
Experimental — accuracy not yet measured
IsdDEF transports heme across the membrane for utilization by IsdG, an orthologue of the S. aureus heme oxygenase.
“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]
IsdG-family heme oxygenases have been characterized in S. lugdunensis, Bacillus anthracis, Bradyrhizobium japonicum, Brucella melitensis, and Mycobacterium tuberculosis.
“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]
IsdG orthologs from these bacteria bind and degrade heme, but they differ in other respects.
“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]

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The Relationship Between Structure and Function of the Heme-Scavenging Protein IsdX1
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ABacillus anthracisS-Layer Homology Protein That Binds Heme and Mediates Heme Delivery to IsdC
Tarlovsky, Y., Fabian, M., Solomaha, E., Honsa, E., Olson, J. S., & Maresso, A. W. (2010) · Journal of Bacteriology · doi:10.1128/jb.00054-10 · Cited by 72 · see citing works

Authors: Skaar, E. P., Gaspar, A. H., & Schneewind, O.
Affiliations: University of Chicago (US)
Corresponding author: Schneewind, Olaf
ORCID: Skaar, Eric P.
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
DOI: 10.1128/jb.188.3.1071-1080.2006
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
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
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 › Cell Biology › 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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Bacillus anthracis IsdG, a Heme-Degrading Monooxygenase

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About these checks