Cited by 58Trypanosoma species research and implicationsResearch on Leishmaniasis StudiesIron Metabolism and Disorders

Trypanosoma cruzi receptors for human transferrin and their role

LIMA, M, VILLALTA, F·1990·Molecular and Biochemical Parasitology

Abstract

Trypanosoma cruzi amastigotes present receptors for human transferrin as indicated by the saturable binding of 125I-transferrin to this form of the parasite. Computerized Scatchard analysis revealed one class of receptors present at 8.1 X 10(4) receptors per amastigote with a Kd of 2.82 microM. Immunofluorescence studies indicate that more than 90% of amastigotes bind human transferrin, whereas trypomastigotes do not. Iron is required for amastigote growth in cell-free medium since deferoxamine, an iron chelator, inhibits amastigote growth. Amastigote growth is restored when deferoxamine is removed from the medium. 59Fe-transferrin, which bound to amastigotes at 4 degrees C for 1 h, was readily dissociated from the parasite surface upon treatment with acid. However, this treatment did not disrupt binding that occurred at 37 degrees C for 1 h. Amastigote growth in cell-free medium is inhibited in ferrotransferrin-depleted serum, and addition of ferrotransferrin but not apotransferrin restores parasite growth. Western blots of solubilized amastigote membranes probed with anti-human transferrin receptor antibody recognize a protein of 200 kDa. This protein is present on the amastigote cell surface; therefore, human transferrin seems to interact with a 200-kDa surface amastigote protein receptor. Iron, which is essential for amastigote growth, thus appears to be delivered to T. cruzi amastigotes by transferrin receptor-mediated endocytosis.

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Crossref · 10.1016/0166-6851(90)90027-j

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  • T. cruzi amastigotes take up Fe-loaded Tf when grown in vitro.

    “The amastigotes of the intracellular parasite Trypanosoma cruzi take up Fe-loaded Tf when grown in vitro, but the physiological significance of this process is unclear [91].”
  • A different mechanism, a different type of transacting factor, is responsible for Fe sensing and regulation of transferrin receptor mRNA in T. brucei.

    “The T. brucei genome contains only one IRP-related gene, which suggests that a different mechanism, a different type of transacting factor, is responsible for Fe sensing and regulation of transferrin receptor mRNA in this protozoan [91, 92].”
  • The T. brucei genome contains only one IRP-related gene.

    “The T. brucei genome contains only one IRP-related gene, which suggests that a different mechanism, a different type of transacting factor, is responsible for Fe sensing and regulation of transferrin receptor mRNA in this protozoan [91, 92].”

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Authors
LIMA, M., & VILLALTA, F.
Affiliations
Meharry Medical College (US)
Corresponding author
VILLALTA, F
Venue
Molecular and Biochemical Parasitology
Publisher
Elsevier BV
Published
1990-01-15
Volume
38
Issue
2
Pages
245-252
ISSN
0166-6851 (ISSN-L)
OpenAlex
W2157517610
Cited by
58
References
25
Citations by year
2026: 2 · 2025: 2 · 2024: 1 · 2023: 1 · 2022: 2 · 2020: 2 · 2018: 1 · 2017: 1 · 2016: 2 · 2015: 3 · 2014: 1 · 2013: 1 · 2012: 2
FWCI
4.10
Type
journal article
Language
en
Open access
closed
Locations
  • Molecular and Biochemical Parasitology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • United States Agency for International Development
  • National Institutes of Health (5r29ai025637-02)
  • U.S. Public Health Service
  • National Institute of Allergy and Infectious Diseases (AI-07181-04, AI-25637-02)
Topics
  • Health Sciences › Medicine › Epidemiology › Trypanosoma species research and implications
  • Health Sciences › Medicine › Public Health, Environmental and Occupational Health › Research on Leishmaniasis Studies
  • Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Keywords
Trypanosoma cruzi, human transferrin, transferrin receptor, amastigotes, iron acquisition, deferoxamine, endocytosis, trypomastigotes, iron chelation, parasite growth
MeSH terms
Animals, Cross Reactions, Deferoxamine, Humans, Iron, Iron Radioisotopes, Protein Binding, Receptors, Transferrin, Transferrin, Trypanosoma cruzi

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