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      Independent translocation of two micronemal proteins in developing Plasmodium falciparum merozoites.

      Infection and Immunity
      Animals, Antigens, Protozoan, Biological Transport, Active, Carrier Proteins, metabolism, Endopeptidases, Erythrocytes, parasitology, Humans, Malaria, Falciparum, etiology, Membrane Proteins, Microscopy, Fluorescence, Microscopy, Immunoelectron, Models, Biological, Organelles, ultrastructure, Plasmodium falciparum, growth & development, pathogenicity, Protein Precursors, Protein Processing, Post-Translational, Protozoan Proteins, Virulence, physiology

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          Abstract

          Apical membrane antigen 1 of Plasmodium falciparum (PfAMA1) contains an N-terminal propeptide that is removed prior to the translocation of the mature protein onto the merozoite surface. We localized unprocessed PfAMA1 to the microneme organelles of the intraerythrocytic schizont. The results have suggested that the processed form of PfAMA1 translocates from the microneme compartment independently of another microneme protein, EBA175, which is also involved in the invasion of human erythrocytes.

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