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J Biol Chem, Vol. 274, Issue 5, 2758-2765, January 29, 1999

Hemoglobin Endocytosis in Leishmania Is Mediated through a 46-kDa Protein Located in the Flagellar Pocket

Shantanu Sengupta, Jalaj Tripathi, Ruchi Tandon, Manoj Raje^§, Rajendra P. Roy, Sandip K. Basu, and Amitabha Mukhopadhyay

From the  National Institute of Immunology, Aruna Asaf Ali Marg, New Delhi 110067 and the ^§ Institute of Microbial Technology, Sector 39A, Chandigarh 160014, India

Four lines of evidence indicate that a specific high affinity binding site on the surface of Leishmania donovani promastigotes mediates rapid internalization and degradation of hemoglobin. 1) Binding and uptake of ¹²⁵I-hemoglobin by Leishmania followed saturation kinetics and were competed by unlabeled hemoglobin but not by globin or hemin or other heme- or iron-containing proteins. 2) Immunogold labeling studies revealed that, at 4 °C, hemoglobin binding was localized in the flagellar pocket of the promastigotes. Indirect immunofluorescence assays showed that, at 37 °C, the bound hemoglobin in such cells entered an endocytic compartment within 2 min and dispersed throughout the cell body by 15 min. 3) After incubation with hemoglobin-gold conjugates at 25 °C or 37 °C, the particles accumulated in discrete intracellular vesicles. 4) A single biotinylated protein of 46 kDa was revealed when solubilized membranes from surface biotinylated intact Leishmania adsorbed by hemoglobin-agarose beads were subjected to SDS-polyacrylamide gel electrophoresis and Western blotting with avidin-horseradish peroxidase. Considered together, these data indicate that this 46-kDa protein on the cell surface of L. donovani promastigotes mediates the binding of hemoglobin and its rapid internalization through a vesicular pathway characteristic of receptor-mediated endocytosis.

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