The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
Intracellular metalloporphyrin metabolism in Staphylococcus aureus
Abstract
The bacterial pathogen Staphylococcus aureus is responsible for a significant amount of human morbidity and mortality, and the ability of S. aureus to cause disease is absolutely dependent on the acquisition of iron from the host. The most abundant iron source to invading staphylococci is in the form of the porphyrin heme. S. aureus is capable of acquiring nutrient iron from heme and hemoproteins via two heme-acquisition systems, the iron-regulated surface determinant system (Isd) and the heme transport system (Hts). Heme acquisition through these systems is involved in staphylococcal pathogenesis suggesting that the intracellular fate of heme plays a significant role in the infectious process. The valuable heme molecule presents a paradox to invading bacteria because although heme is an abundant source of nutrient iron, the extreme reactivity of heme makes it toxic at high concentrations. Therefore, bacteria must regulate the levels of intracellular heme to avoid toxicity. Although the molecular mechanisms responsible for staphylococcal heme acquisition are beginning to emerge, the mechanisms by which S. aureus regulate intracellular heme homeostasis are largely unknown. In this review we describe three potential fates of host-derived heme acquired by S. aureus during infection: (i) degradation for use as a nutrient iron source, (ii) incorporation into bacterial heme-binding proteins for use as an enzyme cofactor, or (iii) efflux through a dedicated ABC-type transport system…
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In the citing paper
“The paradigm for Gram-positive heme uptake is represented by the Staphylococcus aureus i ron-regulated s urface d eterminant system (Isd).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [94]
In the citing paper
“The Isd import machinery is encoded by 10 genes, including four cell wall-anchored proteins (IsdABCH), a transpeptidase (SrtB), a membrane transport system (IsdDEF), and two cytoplasmic heme oxygenases (IsdG and IsdI) (94).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [94]
In the citing paper
“IsdA extracts heme from IsdB or IsdH for passage to IsdC (64, 73, 94, 131).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [94]
In the citing paper
“This efficient heme-scavenging system brings heme across the membrane into the cytoplasm through the IsdDEF ABC transporter, where it can either be degraded by the heme oxygenases IsdG and IsdI to release free iron or be trafficked intact to the cell membrane (68, 94).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [94]
In the citing paper
“Moreover, iron-replete S. aureus preferentially traffics exogenously acquired heme to the cell membrane, although the function of this process is still unknown (94).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [94]
In the citing paper
“The IsdG family of heme oxygenases, first described for S. aureus , degrades heme to release free iron and form staphylobilin in the presence of a reducing agent (94).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [94]
Citations
Cites
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Iron-Source Preference of Staphylococcus aureus Infections
Skaar, E. P., Humayun, M., Bae, T., DeBord, K. L., & Schneewind, O. (2004) · Science · doi:10.1126/science.1099930 · Cited by 440
Self-citationvon Eiff, C., Heilmann, C., Proctor, R. A., Woltz, C., Peters, G., & Götz, F. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.15.4706-4712.1997 · Cited by 310 · cited 2×
“More specifically, S. aureus strains inactivated for hemB are predicted to be unable to form mature cytochromes, yet they are capable of moderate growth rates on solid medium (von Eiff et al. 1997).”
BackgroundStaphylococcus aureus IsdB Is a Hemoglobin Receptor Required for Heme Iron Utilization
Torres, V. J., Pishchany, G., Humayun, M., Schneewind, O., & Skaar, E. P. (2006) · Journal of Bacteriology · doi:10.1128/jb.01335-06 · Cited by 302
Self-citationIsdG and IsdI, Heme-degrading Enzymes in the Cytoplasm of Staphylococcus aureus
Skaar, E. P., Gaspar, A. H., & Schneewind, O. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307952200 · Cited by 282
Self-citationIron uptake mechanisms and their regulation in pathogenic bacteria
Braun, V. (2001) · International Journal of Medical Microbiology · doi:10.1078/1438-4221-00103 · Cited by 249
Schmitt, M. P. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.3.838-845.1997 · Cited by 234
Stojiljkovic, I., Kumar, V., & Srinivasan, N. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01175.x · Cited by 230
Staphylococcus aureus Redirects Central Metabolism to Increase Iron Availability
Friedman, D. B., Stauff, D. L., Pishchany, G., Whitwell, C. W., Torres, V. J., & Skaar, E. P. (2006) · PLoS Pathogens · doi:10.1371/journal.ppat.0020087 · Cited by 222
Self-citationZhu, W., Wilks, A., & Stojiljkovic, I. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.23.6783-6790.2000 · Cited by 186 · cited 7×
“Additional members of this family have been identified in Pseudomonas aeruginosa (PigA) (Ratliff et al. 2001), N. gononrrhoeae (HemO) (Zhu et al. 2000b), and N. meningitides (HemO) ( Zhu et al. 2000b ).”
BackgroundInfluentialWu, R., Skaar, E. P., Zhang, R., Joachimiak, G., Gornicki, P., Schneewind, O., & Joachimiak, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m409526200 · Cited by 144
Self-citationProcessing of Heme and Heme-Containing Proteins by Bacteria
Stojiljkovic, I., & Perkins-Balding, D. (2002) · DNA and Cell Biology · doi:10.1089/104454902753759708 · Cited by 134
Bacillus anthracis IsdG, a Heme-Degrading Monooxygenase
Skaar, E. P., Gaspar, A. H., & Schneewind, O. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.3.1071-1080.2006 · Cited by 123
Self-citationIdentification of an Escherichia coli O157:H7 heme oxygenase with tandem functional repeats
Suits, M. D. L., Pal, G. P., Nakatsu, K., Matte, A., Cygler, M., & Jia, Z. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504289102 · Cited by 91
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Metadata
- Authors
- Reniere, M. L., Torres, V. J., & Skaar, E. P.
- Venue
- BioMetals
- Published
- 2007-03-27
- Volume
- 20
- Issue
- 3-4
- Pages
- 333-345
- ISSN
- 0966-0844
- 1572-8773
- Cited by
- 99
- References
- 16
- Language
- en
- Licence
- www.springer.com/tdm (tdm)
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