The DOI matches its Crossref record; 161 of the 161 references it cites were found in a registry or an index.
Bacterial heme-transport proteins and their heme-coordination modes
Abstract
Efficient iron acquisition is critical for an invading microbe’s survival and virulence. Most of the iron in mammals is incorporated into heme, which can be plundered by certain bacterial pathogens as a nutritional iron source. Utilization of exogenous heme by bacteria involves the binding of heme or hemoproteins to the cell surface receptors, followed by the transport of heme into cells. Once taken into the cytosol, heme is presented to heme oxygenases where the tetrapyrrole ring is cleaved in order to release the iron. Some Gram-negative bacteria also secrete extracellular heme-binding proteins called hemophores, which function to sequester heme from the environment. The heme transport genes are often genetically linked as gene clusters under Fur (Ferric uptake repressor) regulation. This review discusses the gene clusters and proteins involved in bacterial heme acquisition, transport and processing processes, with special focus on the heme coordination, protein structures and mechanisms underlying heme transport.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Under iron-replete conditions, Fur represses the expression of heme uptake machinery in many species, including S. aureus , Y. pestis , and P. aeruginosa (68, 79, 115, 116).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [116]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“The HasA system encodes an export complex (HasDEF), a hemophore receptor (HasR), and regulatory proteins (HasI and HasS) (7, 15, 33, 97, 116).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [116]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Many bacterial pathogens have elegant systems dedicated to the acquisition of heme from host hemoproteins.”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [116]
In the citing paper
“Two types of hemophore-mediated heme uptake systems have been described for Gram-negative bacteria: one uses the HasA hemophore, and the other uses the HxuA hemophore (116).”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [116]
In the citing paper
“Bacterial pathogens can circumvent nearly every vertebrate form of heme sequestration.”
From Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens (2010) · cites this paper as [116]
8 more claims about this paper
Create a free account to see every claim other papers make about this one.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
THE HEME OXYGENASE SYSTEM:A Regulator of Second Messenger Gases
Maines, M. D. (1997) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.37.1.517 · Cited by 2,501
DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae
Heidelberg, J. F., Eisen, J. A., Nelson, W. C., Clayton, R. A., Gwinn, M. L., Dodson, R. J., Haft, D. H., Hickey, E. K., Peterson, J. D., Umayam, L., et al. (2000) · Nature · doi:10.1038/35020000 · Cited by 1,870
Identification of the haemoglobin scavenger receptor
Kristiansen, M., Graversen, J. H., Jacobsen, C., Sonne, O., Hoffman, H.-J., Law, S. K. A., & Moestrup, S. K. (2001) · Nature · doi:10.1038/35051594 · Cited by 1,712
Iron Metabolism in Pathogenic Bacteria
Ratledge, C., & Dover, L. G. (2000) · Annual Review of Microbiology · doi:10.1146/annurev.micro.54.1.881 · Cited by 1,539
Navarre, W. W., & Schneewind, O. (1999) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.63.1.174-229.1999 · Cited by 1,391
Koronakis, V. E., Sharff, A., Koronakis, E., Luisi, B. F., & Hughes, C. (2000) · Nature · doi:10.1038/35016007 · Cited by 1,119
Enterobactin: an archetype for microbial iron transport.
Raymond, K. N., Dertz, E. A., & Kim, S. S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0630018100 · Cited by 933
Bacterial Iron Sources: From Siderophores to Hemophores
Wandersman, C., & Delepelaire, P. (2004) · Annual Review of Microbiology · doi:10.1146/annurev.micro.58.030603.123811 · Cited by 930
The heme synthesis and degradation pathways: role in oxidant sensitivity
Ryter, S. W., & Tyrrell, R. M. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00223-3 · Cited by 831
Mineralization in ferritin: an efficient means of iron storage
Chasteen, N. D., & Harrison, P. M. (1999) · Journal of Structural Biology · doi:10.1006/jsbi.1999.4118 · Cited by 815
Research works printed but not linked: 2
- Bullen, 1978, Curr. Top. Microbiol. Immunol., 80, 1
- Braun, 1995, FEMS Microbiol. Rev., 16, 295, 10.1111/j.1574-6976.1995.tb00177.x · DOI · Paper page
Cited by
Iron in infection and immunity
Cassat, J. E., & Skaar, E. P. (2013) · Cell Host & Microbe · doi:10.1016/j.chom.2013.04.010 · Cited by 1,214
Overcoming the Heme Paradox: Heme Toxicity and Tolerance in Bacterial Pathogens
Anzaldi, L. L., & Skaar, E. P. (2010) · Infection and Immunity · doi:10.1128/iai.00613-10 · Cited by 295
Iron acquisition strategies of bacterial pathogens
Sheldon, J. R., Laakso, H. A., & Heinrichs, D. E. (2016) · Microbiology Spectrum · doi:10.1128/microbiolspec.vmbf-0010-2015 · Cited by 219
Constante, M., Fragoso, G., Calvé, A., Samba-Mondonga, M., & Santos, M. M. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.01809 · Cited by 161
Metal ion acquisition in Staphylococcus aureus: overcoming nutritional immunity
Cassat, J. E., & Skaar, E. P. (2012) · Seminars in Immunopathology · doi:10.1007/s00281-011-0294-4 · Cited by 155
Klebba, P. E., Newton, S. M. C., Six, D. A., Kumar, A., Yang, T., Nairn, B. L., Munger, C., & Chakravorty, S. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01005 · Cited by 150
Role and regulation of heme iron acquisition in gram-negative pathogens
Runyen-Janecky, L. J. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00055 · Cited by 117
Ouattara, M., Bentley Cunha, E., Li, X., Huang, Y., Dixon, D., & Eichenbaum, Z. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07367.x · Cited by 71
Iron-Regulated Surface Determinant (Isd) Proteins of Staphylococcus lugdunensis
Zapotoczna, M., Heilbronner, S., Speziale, P., & Foster, T. J. (2012) · Journal of Bacteriology · doi:10.1128/jb.01195-12 · Cited by 56
Insights on How the Mycobacterium Tuberculosis Heme Uptake Pathway can Be Used as a Drug Target
Owens, C. P., Chim, N., & Goulding, C. W. (2013) · Future Medicinal Chemistry · doi:10.4155/fmc.13.109 · Cited by 50
Hal Is a Bacillus anthracis heme acquisition protein
Balderas, M. A., Nobles, C. L., Honsa, E. S., Alicki, E. R., & Maresso, A. W. (2012) · Journal of Bacteriology · doi:10.1128/jb.00685-12 · Cited by 41
Heme Binding by Corynebacterium diphtheriae HmuT: Function and Heme Environment
Draganova, E. B., Akbas, N., Adrian, S. A., Lukat-Rodgers, G. S., Collins, D. P., Dawson, J. H., Allen, C. E., Schmitt, M. P., Rodgers, K. R., & Dixon, D. W. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00666 · Cited by 26
Iron metabolism: microbes, mouse, and man
Latunde‐Dada, G. O. (2009) · BioEssays · doi:10.1002/bies.200900101 · Cited by 29
Kinetics of heme transfer by the Shr NEAT domains of Group A Streptococcus
Ouattara, M., Pennati, A., Devlin, D. J., Huang, Y.-S., Gadda, G., & Eichenbaum, Z. (2013) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2013.08.009 · Cited by 26
Iron Acquisition Strategies of Bacterial Pathogens
Sheldon, J. R., Laakso, H. A., & Heinrichs, D. E. (2016) · Virulence Mechanisms of Bacterial Pathogens · doi:10.1128/9781555819286.ch3 · Cited by 25
Hariadi, N. I., Zhang, L., Patel, M., Sandstedt, S. A., Davis, G. S., Marrs, C. F., & Gilsdorf, J. R. (2015) · Journal of Clinical Microbiology · doi:10.1128/jcm.00345-15 · Cited by 24
Lee, M. J. Y., Schep, D., McLaughlin, B., Kaufmann, M., & Jia, Z. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.02.013 · Cited by 20
Haemophilus influenzae stores and distributes hemin by using protein E
Al Jubair, T., Singh, B., Fleury, C., Blom, A. M., Mörgelin, M., Thunnissen, M. M., & Riesbeck, K. (2014) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2014.04.015 · Cited by 10
Metadata
- Authors
- Tong, Y., & Guo, M.
- Venue
- Archives of Biochemistry and Biophysics
- Publisher
- Elsevier BV
- Published
- 2009-01
- Volume
- 481
- Issue
- 1
- Pages
- 1-15
- ISSN
- 0003-9861
- PMC
- PMC2683585
- Cited by
- 162
- References
- 161
- Language
- en
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
