ArticlePloS one2012
Heme degrading protein HemS is involved in oxidative stress response of Bartonella henselae.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 21 citations in OpenAlex.
- Insights from a Genome-Wide Study ofCurrent issues in molecular biology · 2025Article
- Vector biology of the cat flea Ctenocephalides felis.Trends in parasitology · 2024Review
- From Host Heme To Iron: The Expanding Spectrum of Heme Degrading Enzymes Used by Pathogenic Bacteria.Frontiers in cellular and infection microbiology · 2018Review
- The Detection of Hemin-Binding Proteins in Riemerella anatipestifer CH-1.Current microbiology · 2016Article
- Insights from the genome annotation of Elizabethkingia anophelis from the malaria vector Anopheles gambiae.PloS one · 2014Article
- Iron homeostasis in theAdvances in botanical research · 2013Article
- Managing iron supply during the infection cycle of a flea borne pathogen, Bartonella henselae.Frontiers in cellular and infection microbiology · 2013Review
- Role and regulation of heme iron acquisition in gram-negative pathogens.Frontiers in cellular and infection microbiology · 2013Review
- Heme binding proteins of Bartonella henselae are required when undergoing oxidative stress during cell and flea invasion.PloS one · 2012Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bartonellae are hemotropic bacteria, agents of emerging zoonoses. These bacteria are heme auxotroph Alphaproteobacteria which must import heme for supporting their growth, as they cannot synthesize it. Therefore, Bartonella genome encodes for a complete heme uptake system allowing the transportation of this compound across the outer membrane, the periplasm and the inner membranes. Heme has been proposed to be used as an iron source for Bartonella since these bacteria do not synthesize a complete system required for iron Fe³⁺ uptake. Similarly to other bacteria which use heme as an iron source, Bartonellae must transport this compound into the cytoplasm and degrade it to allow the release of iron from the tetrapyrrole ring. For Bartonella, the gene cluster devoted to the synthesis of the complete heme uptake system also contains a gene encoding for a polypeptide that shares homologies with heme trafficking or degrading enzymes. Using complementation of an E. coli mutant strain impaired in heme degradation, we demonstrated that HemS from Bartonella henselae expressed in E. coli allows the release of iron from heme. Purified HemS from B. henselae binds heme and can degrade it in the presence of a suitable electron donor, ascorbate or NADPH-cytochrome P450 reductase. Knocking down the expression of HemS in B. henselae reduces its ability to face H₂O₂ induced oxidative stress.
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