BioAcyl Corp
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Soares, M. P., & Weiss, G. (2015). The iron age of host–microbe interactions. EMBO reports, 16(11), 1482–1500. Added by: Dr. Enrique Feoli (14/08/2022, 09:42) Last edited by: Dr. Enrique Feoli (14/08/2022, 09:50) |
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| Resource type: Journal Article DOI: https://doi.org/10.15252/embr.201540558 BibTeX citation key: Soares2015 View all bibliographic details  |
Categories: BioAcyl Corp Subcategories: Microenvironment Creators: Soares, Weiss Collection: EMBO reports |
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| Abstract |
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Abstract Microbes exert a major impact on human health and disease by either promoting or disrupting homeostasis, in the latter instance leading to the development of infectious diseases. Such disparate outcomes are driven by the ever-evolving genetic diversity of microbes and the countervailing host responses that minimize their pathogenic impact. Host defense strategies that limit microbial pathogenicity include resistance mechanisms that exert a negative impact on microbes, and disease tolerance mechanisms that sustain host homeostasis without interfering directly with microbes. While genetically distinct, these host defense strategies are functionally integrated, via mechanisms that remain incompletely defined. Here, we explore the general principles via which host adaptive responses regulating iron (Fe) metabolism impact on resistance and disease tolerance to infection.
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More than 80% of the bioavailable Fe in mammals exists in the form of heme contained in hemoproteins 241. The most abundant pool of Fe in mammals are the prosthetic heme groups of hemoglobin in red blood cells (RBC), followed by the heme groups of myoglobin in muscle cells and those of cytochromes and other ubiquitously expressed hemoproteins in all cells 3854. The Fe required to sustain hemoglobin synthesis is made available by hemophagocytic Mø as these clear senescent RBC by erythrophagocytosis (top right) 49. The heme contained in hemoglobin is transported by heme-responsive gene-1 (HRG1) into the cytoplasm where Fe is extracted by heme-oxygnease-1 (HO-1), exported via ferroportin (FPN), and delivered to traferrin (Tf) in plasma. Surplus cytoplasmic Fe in Mø is incorporated and stored within ferritin. Tf transports and provides Fe to the erythropoietic compartment via TfR, where it is used for heme synthesis (bottom right). Heme synthesis occurs via eight successive enzymatic reactions that take place back and forward in the mitochondria (brown) and the cytosol (blue) Added by: Dr. Enrique Feoli Last edited by: Dr. Enrique Feoli |