Structural biology of heme binding in the Staphylococcus aureus Isd system

Grigg, Jason C.; Ukpabi, Georgia; Gaudin, Catherine F.M.; Murphy, Michael E.P.

doi:10.1016/j.jinorgbio.2009.09.012

Cited by 169Hemoglobin structure and functionIron Metabolism and DisordersBacterial Genetics and Biotechnology

Structural biology of heme binding in the Staphylococcus aureus Isd system

Grigg, Jason C., Ukpabi, Georgia, Gaudin, Catherine F.M., Murphy, Michael E.P.·2010·Journal of Inorganic Biochemistry

DOI 10.1016/j.jinorgbio.2009.09.012

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Abstract

Iron is an absolute requirement for nearly all organisms, but most bacterial pathogens are faced with extreme iron-restriction within their host environments. To overcome iron limitation pathogens have evolved precise mechanisms to steal iron from host supplies. Staphylococcus aureus employs the iron-responsive surface determinant (Isd) system as its primary heme-iron uptake pathway. Hemoglobin or hemoglobin-haptoglobin complexes are bound by Near iron-Transport (NEAT) domains within cell surface anchored proteins IsdB or IsdH. Heme is stripped from the host proteins and transferred between NEAT domains through IsdA and IsdC to the membrane transporter IsdEF for internalization. Once internalized, heme can be degraded by IsdG or IsdI, thereby liberating iron for the organism. Most components of the Isd system have been structurally characterized to provide insight into the mechanisms of heme binding and transport. This review summarizes recent research on the Isd system with a focus on the structural biology of heme recognition.

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Staphylococcus aureus acquires iron through toxin-dependent lysis of red blood cells followed by heme uptake through the iron-regulated surface determinant system.
“S. aureus is well equipped to acquire iron through the toxin-dependent lysis of red blood cells followed by the uptake of heme through the iron-regulated surface determinant (Isd) system (Grigg et al., 2010).”
From The Impact of Dietary Transition Metals on Host-Bacterial Interactions (2018) · cites this paper as Grigg et al., 2010
Iron restriction triggers Fur-regulated virulence factors, including hemolysins that lyse erythrocytes and supply hemoglobin to the Isd system.
“Iron restriction signals entry into host tissues and triggers the secretion of a variety of virulence factors. These virulence factors include hemolysins that increase erthryocyte lysis and supply liberated hemoglobin to the iron regulated surface determinant system (Isd) for use as an iron source [9, 20–22].”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [22]
The Isd system includes cell wall anchored heme binding proteins IsdA and IsdC, hemoglobin receptor IsdB, hemoglobin-haptoglobin receptor IsdH, membrane transporter IsdEF, and cytoplasmic heme oxygenases IsdG and IsdI.
“One such system is the iron regulated surface determinant (Isd) system which includes the cell wall anchored heme binding proteins (IsdA and IsdC), a hemoglobin receptor (IsdB), a hemoglobin-haptoglobin receptor (IsdH), a membrane transporter (IsdEF), and two cytoplasmic heme oxygenases (IsdG and IsdI) [22].”
From A battle for iron: host sequestration and Staphylococcus aureus acquisition (2012) · cites this paper as [22]

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“N IH -PA Author M anuscript N IH -PA Author M anuscript N IH -PA Author M anuscript IsdG and IsdI are 78% similar at the amino acid level yet they are differentially regulated through the proteolytic degradation of apo-IsdG.”
BackgroundInfluential
Surface Proteins ofStaphylococcus aureus
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Mapping Ultra-weak Protein-Protein Interactions between Heme Transporters of Staphylococcus aureus
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The iron-regulated surface determinant B (IsdB) protein from Staphylococcus aureus acts as a receptor for the host protein vitronectin
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The Role of Iron in Staphylococcus aureus Infection and Human Disease: A Metal Tug of War at the Host—Microbe Interface
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Authors: Grigg, J. C., Ukpabi, G., Gaudin, C. F. M., & Murphy, M. E. P.
Affiliations: University of British Columbia (CA)
Corresponding author: Murphy, Michael E.P.
ORCID: Grigg, Jason C.
Murphy, Michael E.P.
Venue: Journal of Inorganic Biochemistry
Publisher: Elsevier BV
Published: 2010-03
Volume: 104
Issue: 3
Pages: 341-348
ISSN: 0162-0134 (ISSN-L)
DOI: 10.1016/j.jinorgbio.2009.09.012
OpenAlex: W2086406020
Cited by: 169
References: 74
Citations by year: 2026: 10 · 2025: 14 · 2024: 9 · 2023: 5 · 2022: 8 · 2021: 3 · 2020: 6 · 2019: 7 · 2018: 8 · 2017: 14 · 2016: 13 · 2015: 12 · 2014: 12 · 2013: 14 · 2012: 16
FWCI: 5.04
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Journal of Inorganic Biochemistry (publishedVersion)
PubMed (publishedVersion)
Funders: Canadian Institutes of Health Research (MOP-49597)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords: Staphylococcus aureus, heme binding, iron acquisition, NEAT domain, ISDB, IsdH, ISDA, IsdC, heme degradation, hemoglobin, haptoglobin, iron limitation, pathogenic bacteria, protein structure
MeSH terms: Amino Acid Sequence, Bacterial Proteins, Biological Transport, Cell Wall, Haptoglobins, Heme, Hemoglobins, Iron, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Conformation, Staphylococcus aureus, Molecular Structure, Sequence Alignment, Crystallography, X-Ray

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Structural biology of heme binding in the Staphylococcus aureus Isd system

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