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Cited by 56Research on Leishmaniasis StudiesTrypanosoma species research and implicationsIron Metabolism and Disorders

Leishmania chagasi: uptake of iron bound to lactoferrin or transferrin requires an iron reductase

Wilson, Mary E., Lewis, Troy S., Miller, Melissa A., McCormick, Michael L., Britigan, Bradley E.·2002·Experimental Parasitology
DOI 10.1016/s0014-4894(02)00018-8
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Abstract

Leishmania chagasi can utilize iron bound to transferrin, lactoferrin, or other chelates. We investigated the mechanism of iron uptake. Promastigotes preferentially took up iron in a reduced rather than an oxidized form, suggesting that extracellular iron must be reduced prior to internalization. Similar to literature reports, a 70-kDa protein in promastigote membrane-containing microsomes bound to [125I]-labeled transferrin. However, [125I]lactoferrin and [125I]albumin also bound a similar 70-kDa protein, suggesting that binding might not be specific. Both total and fractionated promastigotes exhibited an NADPH-dependent iron reductase activity. In contrast to trypanosomes, which take up transferrin through a specific receptor, these data support a model in which a parasite-associated or secreted reductase reduces ferric to ferrous iron, decreasing its affinity for the extracellular chelate and allowing it to be readily internalized by the parasite. This could account for the ability of the parasite to utilize iron from multiple sources in diverse host environments. Index Descriptors and Abbreviations. Index descriptors: Cryptococcus neoformans, Histoplasma capsulatum, iron, iron reductase, lactoferrin, L. chagasi, leishmaniasis, nutrient acquisition, protozoan, Saccharomyces cerevisiae, Trypanosoma brucei, Trypanosoma cruzi, transferrin; Abbreviations used: DNA, deoxyribonucleic acid; DTT, dithiothreitol; HBSS, Hanks' balanced salt solution; MTT, 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide; NEM, N-ethylmaleimide; RNA, ribonucleic acid.

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57 of 57 references verified0 citation errors · 0 not checkable

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  • Leishmania strips iron of TF and LF before its reduction by LFR1 and uptake as ferrous iron via LIT1.

    “In addition, Leishmania strips iron of TF and LF before its reduction by LFR1 (for Leishmania ferric reductase-1) and uptake as ferrous iron via LIT1 (for Leishmania ferrous iron transporter-1) (Flannery et al., 2011;Miguel et al., 2013;Wilson et al., 2002).”

    From Iron in infection and immunity (2020) · cites this paper as Wilson et al., 2002

  • In addition to Tf, growth and survival of L. infantum and L. amazonensis amastigotes can be supported by Fe derived from hemoglobin and hemin.

    “In addition to Tf, the growth and survival of L. infantum and L. amazonensis amastigotes can be supported by Fe derived from hemoglobin and hemin [83].”

    From Strategies of intracellular pathogens for obtaining iron from the environment (2015) · cites this paper as [83]

  • Intracellular L. amazonensis possesses a ferric reductase, LFR1, which provides soluble Fe2+ for transport across the parasite plasma membrane by LIT1.

    “Furthermore, intracellular L. amazonensis also possesses a ferric reductase, the Leismania ferric iron reductase 1 (LFR1), which provides soluble Fe2+ for transport across the parasite plasma membrane by the ferrous iron transporter, Leishmania iron transporter 1 (LIT1) [83, 84].”

    From Strategies of intracellular pathogens for obtaining iron from the environment (2015) · cites this paper as [83]

  • Uptake of heme by intramacrophagic L. amazonensis amastigotes is mediated by the Leishmania heme response 1 (LHR1) protein.

    “The uptake of heme by intramacrophagic L. amazonensis amastigotes is mediated by the Leishmania heme response 1 (LHR1) protein.”

    From Strategies of intracellular pathogens for obtaining iron from the environment (2015) · cites this paper as [83]

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Authors
Wilson, M. E., Lewis, T. S., Miller, M. A., McCormick, M. L., & Britigan, B. E.
Affiliations
University of Iowa (US)
Corresponding author
Wilson, Mary E.
ORCID
Venue
Experimental Parasitology
Publisher
Elsevier BV
Published
2002-03
Volume
100
Issue
3
Pages
196-207
ISSN
0014-4894 (ISSN-L)
DOI
10.1016/s0014-4894(02)00018-8
OpenAlex
W2023127335
Cited by
56
References
58
Citations by year
2026: 1 · 2025: 1 · 2024: 1 · 2023: 2 · 2022: 4 · 2021: 1 · 2020: 3 · 2019: 4 · 2018: 2 · 2017: 1 · 2016: 3 · 2015: 3 · 2014: 1 · 2013: 5 · 2012: 2
FWCI
1.40
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Experimental Parasitology (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Institute of Allergy and Infectious Diseases (R01AI034954, AI-34954, R01AI045540, AI 32135, AI 45540)
Topics
  • Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Research on Leishmaniasis Studies
  • Health Sciences › Medicine › Epidemiology › Trypanosoma species research and implications
  • Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Keywords
Leishmania infantum, iron absorption, iron reductase, lactoferrin, transferrin, Fe(III) reduction, promastigotes, NADPH-dependent reductase, iron chelates, nutrient acquisition, leishmaniasis
MeSH terms
Animals, Cricetinae, Iodine Radioisotopes, Iron, Lactoferrin, Ligands, Mesocricetus, NADH, NADPH Oxidoreductases, Transferrin, Protozoan Proteins, Leishmania infantum, FMN Reductase

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