Staphylococcus lugdunensis IsdG Liberates Iron from Host Heme
Open accessAbstract
Staphylococcus lugdunensis is often found as part of the normal flora of human skin but has the potential to cause serious infections even in healthy individuals. It remains unclear what factors enable S. lugdunensis to transition from a skin commensal to an invasive pathogen. Analysis of the complete genome reveals a putative iron-regulated surface determinant (Isd) system encoded within S. lugdunensis. In other bacteria, the Isd system permits the utilization of host heme as a source of nutrient iron to facilitate bacterial growth during infection. In this study, we establish that S. lugdunensis expresses an iron-regulated IsdG-family heme oxygenase that binds and degrades heme. Heme degradation by IsdG results in the release of free iron and the production of the chromophore staphylobilin. IsdG-mediated heme catabolism enables the use of heme as a sole source of iron, establishing IsdG as a pathophysiologically relevant heme oxygenase in S. lugdunensis. Together these findings offer insight into how S. lugdunensis fulfills its nutritional requirements while invading host tissues and establish the S. lugdunensis Isd system as being involved in heme-iron utilization.
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Many other pathogens have evolved NEAT-containing heme acquisition systems, including Staphylococcus lugdunensis, L. monocytogenes, and Streptococcus pyogenes.
“In addition to S. aureus and B. anthracis, many other pathogens have evolved NEAT-containing heme acquisition systems, including Staphylococcus lugdunensis, L. monocytogenes, and Streptococcus pyogenes [136–143].”
From Heme Synthesis and Acquisition in Bacterial Pathogens (2016) · cites this paper as [138]
S. lugdunensis IsdB contains an aromatic motif identical to the one described here.
“In particular, S. lugdunensis IsdB contains an aromatic motif that is identical to the one described here .”
From IsdB-dependent hemoglobin binding is required for acquisition of heme by Staphylococcus aureus (2014) · cites this paper as [41]
Staphylococcus lugdunensis has an Isd system highly similar to that of S. aureus.
“Another staphylococcal pathogen, Staphylococcus lugdunensis , encodes an Isd system that is highly similar to that of S. aureus [41, 42] .”
From IsdB-dependent hemoglobin binding is required for acquisition of heme by Staphylococcus aureus (2014) · cites this paper as [41]
S. lugdunensis has a single IsdG-family heme oxygenase that is iron regulated.
“S. lugdunensis encodes a single IsdG-family heme oxygenase which is iron regulated.”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [50]
Some bacteria that contain IsdG are extremophiles living in very harsh environments.
“In fact, some of these IsdG-containing bacteria are considered extremophiles, occupying some of the earth's harshest environments.”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [50]
All IsdG-encoding extremophiles also carry a putative heme synthesis pathway.
“Interestingly, genomic analysis reveals that all IsdG encoding extremophiles also encode for a putative heme synthesis pathway.”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [50]
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 [50]
S. lugdunensis IsdG and S. aureus IsdG are 68% identical in amino acid sequence, but the S. lugdunensis enzyme remains stable without heme.
“Although S. lugdunensis IsdG and S. aureus IsdG are 68% identical at the amino acid level the S. lugdunensis enzyme is stable in the absence of heme.”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [50]
Many bacterial species carrying a putative IsdG have no known plant or animal host from which they could obtain heme.
“A recent survey of annotated bacterial genomes uncovered that many bacterial species which encode for a putative IsdG have no known association with any plant or animal from which they could acquire heme [50].”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [50]
Staphylobilin production by IsdG-family enzymes is not limited to Staphylococcus aureus.
“Studies into IsdG from S. lugdunensis, a pathogenic coagulase-negative staphylococci, have revealed that staphylobilin production by IsdG family members is not restricted to S. aureus [50].”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [50]
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 [50]
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Sekar, S., Schwarzbach, S., Nega, M., Bloes, D. A., Smeds, E., Kretschmer, D., Foster, T. J., & Heilbronner, S. (2024) · The FASEB Journal · doi:10.1096/fj.202400335r · Cited by 2 · see citing works
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Haley, K. P. (2014)
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- Authors
- Haley, K. P., Janson, E. M., Heilbronner, S., Foster, T. J., & Skaar, E. P.
- Affiliations
- Vanderbilt University Medical Center (US)
- Vanderbilt University (US)
- Trinity College Dublin (IE)
- Corresponding author
- Skaar, Eric P.
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 2011-09-15
- Volume
- 193
- Issue
- 18
- Pages
- 4749-4757
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- PMC
- PMC3165669
- OpenAlex
- W2164777902
- Cited by
- 53
- References
- 42
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 2 · 2023: 3 · 2022: 4 · 2021: 2 · 2020: 3 · 2019: 4 · 2018: 1 · 2017: 1 · 2016: 6 · 2015: 4 · 2014: 5 · 2013: 6 · 2012: 6
- FWCI
- 3.85
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Journal of Bacteriology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Arrow@dit (Dublin Institute of Technology) (submittedVersion)
- Funders
- Vanderbilt University
- Irish Research Council for Science, Engineering and Technology
- Science Foundation Ireland
- U.S. Public Health Service (5 T32 A107611-10)
- National Institute of Allergy and Infectious Diseases (AI073843, AI69233, R01AI069233, R01AI073843)
- Topics
- Health Sciences › Medicine › Infectious Diseases › Antimicrobial Resistance in Staphylococcus
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Keywords
- Staphylococcus lugdunensis, heme oxygenase, bacterial pathogenesis, bacterial iron metabolism
- MeSH terms
- Amino Acid Sequence, Heme, Humans, Iron, Molecular Sequence Data, Oxidation-Reduction, Oxygenases, Phylogeny, Sequence Alignment, Sequence Homology, Amino Acid, Staphylococcus lugdunensis
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