Iron-Regulated Surface Determinant (Isd) Proteins of Staphylococcus lugdunensis

Zapotoczna, Marta; Heilbronner, Simon; Speziale, Pietro; Foster, Timothy J.

doi:10.1128/jb.01195-12

Cited by 56Antimicrobial Resistance in StaphylococcusBacterial Genetics and BiotechnologyBiochemical and Structural Characterization

Iron-Regulated Surface Determinant (Isd) Proteins of Staphylococcus lugdunensis

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Zapotoczna, Marta, Heilbronner, Simon, Speziale, Pietro, Foster, Timothy J.·2012·Journal of Bacteriology

DOI 10.1128/jb.01195-12PMC PMC3497513

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Abstract

Staphylococcus lugdunensis is the only coagulase-negative Staphylococcus species with a locus encoding iron-regulated surface determinant (Isd) proteins. In Staphylococcus aureus , the Isd proteins capture heme from hemoglobin and transfer it across the wall to a membrane-bound transporter, which delivers it into the cytoplasm, where heme oxygenases release iron. The Isd proteins of S. lugdunensis are expressed under iron-restricted conditions. We propose that S. lugdunensis IsdB and IsdC proteins perform the same functions as those of S. aureus . S. lugdunensis IsdB is the only hemoglobin receptor within the isd locus. It specifically binds human hemoglobin with a dissociation constant ( K d ) of 23 nM and transfers heme on IsdC. IsdB expression promotes bacterial growth in an iron-limited medium containing human hemoglobin but not mouse hemoglobin. This correlates with weak binding of IsdB to mouse hemoglobin in vitro . Unlike IsdB and IsdC, the proteins IsdJ and IsdK are not sorted to the cell wall in S. lugdunensis . In contrast, IsdJ expressed in S. aureus and Lactococcus lactis is anchored to peptidoglycan, suggesting that S. lugdunensis sortases may differ in signal recognition or could be defective. IsdJ and IsdK are present in the culture supernatant, suggesting that they could acquire heme from the external milieu. The IsdA protein of S. aureus protects bacteria from bactericidal lipids due to its hydrophilic C-terminal domain. IsdJ has a similar region and protected S. aureus and L. lactis as efficiently as IsdA but, possibly due to its location, was less effective in its natural host.

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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 [137]
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 [42]
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 [42]
IsdB from both species prefers human hemoglobin over mouse hemoglobin.
“IsdB from both species displays a preference for human hemoglobin over mouse hemoglobin, which has important implications for the evolution of these organisms to infect their primary host [29, 42].”
From IsdB-dependent hemoglobin binding is required for acquisition of heme by Staphylococcus aureus (2014) · cites this paper as [42]

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Staphylococcus aureus IsdB Is a Hemoglobin Receptor Required for Heme Iron Utilization
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Authors: Zapotoczna, M., Heilbronner, S., Speziale, P., & Foster, T. J.
Affiliations: Trinity College Dublin (IE)
University of Pavia (IT)
ORCID: Zapotoczna, Marta
Heilbronner, Simon
Speziale, Pietro
Foster, Timothy J.
Venue: Journal of Bacteriology
Publisher: American Society for Microbiology
Published: 2012-12
Volume: 194
Issue: 23
Pages: 6453-6467
ISSN: 0021-9193 (ISSN-L)
1098-5530
DOI: 10.1128/jb.01195-12
PMC: PMC3497513
OpenAlex: W2108095276
Semantic Scholar: b54bd5dac313be45deec66f623f45b0f0793c257
Cited by: 56
References: 78
Citations by year: 2026: 2 · 2025: 4 · 2024: 5 · 2023: 1 · 2022: 4 · 2021: 2 · 2020: 6 · 2019: 3 · 2018: 2 · 2017: 4 · 2016: 7 · 2015: 3 · 2014: 7 · 2013: 6
FWCI: 3.55
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Journal of Bacteriology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Arrow@dit (Dublin Institute of Technology) (submittedVersion, cc-by-nc-sa)
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 › Molecular Biology › Biochemical and Structural Characterization
Keywords: Staphylococcus lugdunensis, ISDB, IsdC, ISDA, heme acquisition, hemoglobin binding, iron limitation, sortase, coagulase-negative staphylococci, Staphylococcus aureus
MeSH terms: Animals, Bacterial Proteins, Culture Media, Hemoglobins, Humans, Iron, Membrane Proteins, Protein Binding, Staphylococcus aureus, Lactococcus lactis, Gene Expression Regulation, Bacterial, Mice, Staphylococcus lugdunensis

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Iron-Regulated Surface Determinant (Isd) Proteins of Staphylococcus lugdunensis

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