Transferrin Binding Proteins as a Means to Obtain Iron in Parasitic Protozoa

Reyes-López, Magda; Serrano-Luna, Jesús; Piña-Vázquez, Carolina; Garza, Mireya de la

doi:10.5772/48288

Cited by 3 publications

(5 citation statements)

References 168 publications

(243 reference statements)

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“…These mechanisms include the secretion of specific Tf proteases, the presence of reductases that capture host Fe-containing proteins, or through specific TfR or Tf binding proteins [ 29 ]. The presence of TfR to piracy Fe must be effective enough to ensure parasites pathogenic potential and proliferation.…”

Section: Tfr In Protozoan Parasitic Organismsmentioning

confidence: 99%

Transferrin: Endocytosis and Cell Signaling in Parasitic Protozoa

Reyes-López

Piña-Vázquez

Serrano-Luna

2015

BioMed Research International

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Iron is the fourth most abundant element on Earth and the most abundant metal in the human body. This element is crucial for life because almost all organisms need iron for several biological activities. This is the case with pathogenic organisms, which are at the vanguard in the battle with the human host for iron. The latest regulates Fe concentration through several iron-containing proteins, such as transferrin. The transferrin receptor transports iron to each cell that needs it and maintains it away from pathogens. Parasites have developed several strategies to obtain iron as the expression of specific transferrin receptors localized on plasma membrane, internalized through endocytosis. Signal transduction pathways related to the activation of the receptor have functional importance in proliferation. The study of transferrin receptors and other proteins with action in the signaling networks is important because these proteins could be used as therapeutic targets due to their specificity or to differences with the human counterpart. In this work, we describe proteins that participate in signal transduction processes, especially those that involve transferrin endocytosis, and we compare these processes with those found in T. brucei, T. cruzi, Leishmania spp., and E. histolytica parasites.

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Section: Tfr In Protozoan Parasitic Organismsmentioning

confidence: 99%

Transferrin: Endocytosis and Cell Signaling in Parasitic Protozoa

Reyes-López

Piña-Vázquez

Serrano-Luna

2015

BioMed Research International

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“…T. gondii utilize iron bound to inorganic or organic chelates, such as serum Lf and transferrin and/or intracellular iron compounds (Hb, hemin, ferritin and others [555,556] . Iron uptake by the parasite was limited by IFN-γ through an unknown mechanism [518] . Dziadek et al [557] found in human CaCo-2 epithelial cells, and mouse L929 fibroblasts, that extracellular T. gondii tachyzoites of BK strain (genotype I) bind specifically human serum Lf but not transferrin, and the binding was concentration-dependent.…”

Section: T Gondii Infectionmentioning

confidence: 99%

“…Moreover, the multiplication of the parasite was inhibited by human Lf high concentrations (≥ 100 mg/ mL) in both cell lines [553] . Virtually all cells express a transferrin receptor on their surface, and the quantity of receptor molecules reflects the cellular iron requirements [518] . It should be noted that host cell expression of transferrin receptor was upregulated in T. gondii infected cells, suggesting that the parasite utilized the host endocytic pathway for iron acquisition [518,526] .…”

Section: T Gondii Infectionmentioning

confidence: 99%

“…Virtually all cells express a transferrin receptor on their surface, and the quantity of receptor molecules reflects the cellular iron requirements [518] . It should be noted that host cell expression of transferrin receptor was upregulated in T. gondii infected cells, suggesting that the parasite utilized the host endocytic pathway for iron acquisition [518,526] . Since the receptors for human Lf also are expressed on many human cells, they could provide a mechanism for the interaction between Lf binding T. gondii tachyzoites and host cells [558] .…”

Section: T Gondii Infectionmentioning

confidence: 99%

“…Hydroxyl radicals can depolymerize polysaccharides, cause DNA breaks, inactivate enzymes, and initiate lipid peroxidation [160,[515][516][517] . Extracellular ferric anion is bound to human serum lactoferrin (Lf) and transferrin, and transferrin is the iron transporter that allows cellular iron uptake [518] . Lf and transferrin maintain Fe 3+ in a soluble and stable oxidation state, avoiding the generation of toxic free hydroxyl radicals [514] .…”

Section: Atherosclerosismentioning

confidence: 99%

See 2 more Smart Citations

Possible Pivotal Role of Latent Chronic T. gondii Infection in the Pathogenesis of Atherosclerosis

Prandota

2017

Journal of Cardiology and Therapy

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Protective Response Against Acinetobacter Baumannii with Ferric Iron Receptors Hemtr-Baua in a Murine Sepsis Model

2021

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Aim: Iron uptake and metabolism pathways are promising targets in vaccine development as an alternative strategy for antibiotics. Methods & methods: HemTR, a putative heme receptor of Acinetobacter baumannii, was expressed and its protectivity against A. baumannii was determined singly or in combination with the siderophore receptor, BauA, in mice. Results: High level of IgG was elicited. There was a delay in mice mortality with reduced bacterial loads in internal organs in the sublethal challenge. Protection was better in the HemTR-BauA group in both lethal and sublethal challenges. Passive transfer of anti-HemTR and anti-BauA partially protected mice against A. baumannii infection. Conclusion: HemTR in combination with other iron receptors could contribute to the development of protective vaccines against A. baumannii.

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Transferrin Binding Proteins as a Means to Obtain Iron in Parasitic Protozoa

Cited by 3 publications

References 168 publications

Transferrin: Endocytosis and Cell Signaling in Parasitic Protozoa

Transferrin: Endocytosis and Cell Signaling in Parasitic Protozoa

Possible Pivotal Role of Latent Chronic T. gondii Infection in the Pathogenesis of Atherosclerosis

Protective Response Against Acinetobacter Baumannii with Ferric Iron Receptors Hemtr-Baua in a Murine Sepsis Model

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