Bacterial transferrin receptors ? structure, function and contribution to virulence

Williams, Paul; Griffiths, Elwyn

doi:10.1007/bf00191543

Cited by 79 publications

(90 citation statements)

References 108 publications

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“…This is supported by reports that describe a membrane-associated flavin reductase in S. mutans that reduces ferric (III) iron into its more soluble ferrous (II) form prior to internalization (Evans et al, 1986). A transferrin receptor has not yet been identified in S. mutans, however, nor has one been described in other Gram-positive pathogens known to utilize transferrin as an iron source (Williams & Griffiths, 1992).…”

Section: Discussionmentioning

confidence: 89%

Expression of Streptococcus mutans fimA is iron-responsive and regulated by a DtxR homologue

et al. 2001

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Iron uptake, transport and storage in Streptococcus mutans, the principal causative agent of human dental cavities, is unexplored despite early reports in the literature which predict a role for this trace metal in cariogenesis. Experiments in the authors' laboratory revealed several iron-responsive proteins in S. mutans, one of which reacted with a polyclonal antiserum directed against the FimA fimbrial adhesin from Streptococcus parasanguis on Western blots. The results of Western blot and Northern hybridization experiments support an inverse relationship between iron availability and S. mutans fimA expression, and metal ion uptake experiments implicate FimA in S. mutans 55 Fe transport. Cloning of the S. mutans fimA homologue facilitated the construction of a fimA knockout mutant which grew poorly in an ironlimiting medium relative to the wild-type progenitor strain, lending further support to a role for FimA in S. mutans iron transport. The authors also identified and cloned a dtxR-like gene (dlg) located downstream of fimA on the S. mutans chromosome, and noted increased fimA expression in a S. mutans dlg knockout mutant relative to wild-type on RNA spot blots and Western blots. The uptake of 55 Fe, which was also significantly increased in this mutant, was compromised in a fimA/dlg double knockout. These findings are consistent with a role for Dlg in the iron-mediated regulation of fimA, and possibly other S. mutans iron transporters. Finally, the cariogenic potential of the fimA and dlg knockout mutants was not significantly different from that of the wild-type progenitor in a germ-free rat model.

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Section: Discussionmentioning

confidence: 89%

Expression of Streptococcus mutans fimA is iron-responsive and regulated by a DtxR homologue

et al. 2001

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“…iV iron bypasses the physiologic controls of iron absorption and storage, thereby exposing the patient to higher levels of circulating free iron and higher tissue levels of iron. a number of authors recently reviewed the link between free or stored iron and a variety of disease states, including cardiovascular disease (18,22), carcinogenesis (19,23) and infection (15,24). the chemical and microbiological quality of water used in dialysate plays a crucial role in the mortality and morbidity of patients on hd.…”

Section: Discussionmentioning

confidence: 99%

Effectiveness of oral iron to manage anemia in long-term hemodialysis patients with the use of ultrapure dialysate

Tsuchida¹,

Paudyal²,

Paudyal

et al. 2010

Experimental and Therapeutic Medicine

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Abstract. the aim of this study was to evaluate the effectiveness of oral iron to manage anemia in long-term hemodialysis (hd) patients using ultrapure dialysate. this study was prospectively conducted on 23 patients (11 males and 12 females; median age 60 years, range 35-81) who underwent hd in our hospital from march to September 2007. the patients were randomly assigned to two treatment groups. The first group of 11 patients received ferrous fumarate 305 mg per oral tablet once a day, while the second group of 12 patients received infusions of 50 mg iron in a 0.9% sodium chloride solution. at the end of the 6-month treatment, patients receiving oral iron and intravenous iron had a significant increase in transferrin saturation from baseline (20.1±8.9 to 29.7±7.2; p=0.011 and 17.4±6.1 to 33.7±8.6; p=0.0001, respectively) and ferritin (32.6±15.4 to 115.4±28.2; p=0.0001 and 57.8±26.7 to 183.5±47.5; p=0.0002, respectively). in both groups, hemoglobin, hematocrit and dry weight were increased, but did not reach statistical significance. Moreover, both groups showed a significant reduction in the mean weekly erythropoietin dose from baseline (5,590.9±1,513.6 to 3,727.3±1,618.1; p=0.011 and 6,775.8±2,292.2 to 4,375.0±2,473.7; p=0.027, respectively). Oral iron is indeed as effective as intravenous iron in managing anemia in hd patients using ultrapure dialysate.

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“…Several pathogens including Staphylococcus aureus, S. epidermidis, N. meningitidis, N. gonorrhoeae, H. influenza and others are known to acquire iron by the direct binding of transferrin on the cell surface [21][22][23][24] . However, no in vivo or in vitro studies have ever identified the existence of transferrin-binding proteins on the surface of M.tb.…”

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confidence: 99%

Mycobacterium tuberculosis acquires iron by cell-surface sequestration and internalization of human holo-transferrin

et al. 2014

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Mycobacterium tuberculosis (M.tb), which requires iron for survival, acquires this element by synthesizing iron-binding molecules known as siderophores and by recruiting a host iron-transport protein, transferrin, to the phagosome. The siderophores extract iron from transferrin and transport it into the bacterium. Here we describe an additional mechanism for iron acquisition, consisting of an M.tb protein that drives transport of human holo-transferrin into M.tb cells. The pathogenic strain M.tb H37Rv expresses several proteins that can bind human holo-transferrin. One of these proteins is the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH, Rv1436), which is present on the surface of M.tb and its relative Mycobacterium smegmatis. Overexpression of GAPDH results in increased transferrin binding to M.tb cells and iron uptake. Human transferrin is internalized across the mycobacterial cell wall in a GAPDH-dependent manner within infected macrophages.

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Bacterial transferrin receptors ? structure, function and contribution to virulence

Cited by 79 publications

References 108 publications

Expression of Streptococcus mutans fimA is iron-responsive and regulated by a DtxR homologue

Expression of Streptococcus mutans fimA is iron-responsive and regulated by a DtxR homologue

Effectiveness of oral iron to manage anemia in long-term hemodialysis patients with the use of ultrapure dialysate

Mycobacterium tuberculosis acquires iron by cell-surface sequestration and internalization of human holo-transferrin

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