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Related Experiment Videos

The transferrin receptor in African trypanosomes: identification, partial characterization and subcellular

D J Grab1, M K Shaw, C W Wells

  • 1International Laboratory for Research on Animal Diseases, Nairobi/Kenya.

European Journal of Cell Biology
|October 1, 1993
PubMed
Summary

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African trypanosomes need iron, acquired via transferrin (Tf) endocytosis. Researchers identified a novel 90 kDa Tf-binding protein in Trypanosoma brucei brucei, likely acting as the parasite's iron receptor.

Area of Science:

  • Parasitology
  • Molecular Biology
  • Cell Biology

Background:

  • Eukaryotic cells, including African trypanosomes, require iron for essential functions like growth and division.
  • Iron uptake in trypanosomes occurs through receptor-mediated endocytosis of iron-loaded transferrin (diFe(3+)-transferrin).
  • Unlike mammalian cells, transferrin (Tf) in trypanosomes is typically delivered to lysosomes and may not recycle to the cell surface.

Purpose of the Study:

  • To characterize a transferrin (Tf)-binding protein with receptor-like properties in Trypanosoma brucei brucei.
  • To identify the molecular mass and binding characteristics of this Tf-binding protein.
  • To determine the localization of the Tf-binding protein within the parasite and its role in iron acquisition.

Main Methods:

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  • Incubation of bloodstream forms of T. brucei with [35S]methionine.
  • Chromatography of detergent lysates on Sephacryl S-300 columns.
  • Immunoprecipitation of Tf/Tf-binding protein complexes using anti-Tf serum.
  • Isolation of Tf-binding proteins using diferric Tf-Sepharose.
  • Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) for molecular mass determination.
  • Raising antisera against T. brucei Tf-binding proteins and Western blot analysis.
  • Immunolocalization studies using specific antisera.

    • Main Results:

    • A major Tf-binding protein with a molecular mass of 88-92 kDa was identified.
    • Further analysis indicated a molecular mass of approximately 90 kDa for the Tf-binding protein.
    • Each 90 kDa Tf-binding protein molecule was found to bind one molecule of diferric Tf.
    • Antibodies against the T. brucei Tf-binding protein inhibited parasite growth in vitro.
    • Immunolocalization revealed the protein resides in the flagellar pocket and early endosomal compartments, with additional presence in lysosomes under specific conditions.

    Conclusions:

    • A 90 kDa Tf-binding protein in T. brucei exhibits receptor-like properties.
    • This protein is a strong candidate for the physiological receptor mediating transferrin uptake in these parasites.
    • The localization suggests a role in the endocytic pathway for iron acquisition.