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Cited by 34Bacillus and Francisella bacterial researchBacterial Genetics and BiotechnologyIron Metabolism and Disorders

Cellular Iron Distribution in Bacillus anthracis

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Tu, W. Y., Pohl, S., Gray, J., Robinson, N. J., Harwood, C. R., Waldron, K. J.·2012·Journal of Bacteriology
DOI 10.1128/jb.06195-11PMC PMC3294808
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Abstract

Although successful iron acquisition by pathogens within a host is a prerequisite for the establishment of infection, surprisingly little is known about the intracellular distribution of iron within bacterial pathogens. We have used a combination of anaerobic native liquid chromatography, inductively coupled plasma mass spectrometry, principal-component analysis, and peptide mass fingerprinting to investigate the cytosolic iron distribution in the pathogen Bacillus anthracis. Our studies identified three of the major iron pools as being associated with the electron transfer protein ferredoxin, the miniferritin Dps2, and the superoxide dismutase (SOD) enzymes SodA1 and SodA2. Although both SOD isozymes were predicted to utilize manganese cofactors, quantification of the metal ions associated with SodA1 and SodA2 in cell extracts established that SodA1 is associated with both manganese and iron, whereas SodA2 is bound exclusively to iron in vivo. These data were confirmed by in vitro assays using recombinant protein preparations, showing that SodA2 is active with an iron cofactor, while SodA1 is cambialistic, i.e., active with manganese or iron. Furthermore, we observe that B. anthracis cells exposed to superoxide stress increase their total iron content more than 2-fold over 60 min, while the manganese and zinc contents are unaffected. Notably, the acquired iron is not localized to the three identified cytosolic iron pools.

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  • In Bacillus anthracis, the manganese metalloproteome is dominated by a single enzyme, MnSOD.

    “In Bacillus anthracis, the manganese metalloproteome is dominated by a single enzyme, the manganese superoxide dismutase (MnSOD).104”

    From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [104]

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Authors
Tu, W. Y., Pohl, S., Gray, J., Robinson, N. J., Harwood, C. R., & Waldron, K. J.
Affiliations
Newcastle University (GB)
ORCID
Venue
Journal of Bacteriology
Publisher
American Society for Microbiology
Published
2011-12-16
Volume
194
Issue
5
Pages
932-940
ISSN
0021-9193 (ISSN-L)
DOI
10.1128/jb.06195-11
PMC
PMC3294808
OpenAlex
W1987789768
Cited by
34
References
6
Citations by year
2026: 3 · 2025: 2 · 2024: 1 · 2023: 1 · 2022: 2 · 2020: 2 · 2018: 5 · 2017: 2 · 2016: 4 · 2015: 2 · 2014: 2 · 2013: 1 · 2012: 5
FWCI
1.22
Type
journal article
Language
en
Open access
Locations
  • Journal of Bacteriology (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Newcastle University ePrints (Newcastle Univesity)
Funders
  • European Commission (LSHG-CT-2006-037469)
  • Biotechnology and Biological Sciences Research Council (P18581, BB/E001688/1)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bacillus and Francisella bacterial research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Keywords
Bacillus anthracis, ferredoxin, superoxide dismutase, manganese cofactor, iron cofactor, superoxide stress, iron acquisition, bacterial metal homeostasis
MeSH terms
Bacillus anthracis, Bacterial Proteins, Chromatography, Liquid, Cytosol, DNA-Binding Proteins, Ferredoxins, Iron, Peptide Mapping, Protein Binding, Mass Spectrometry, Superoxide Dismutase

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