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Primary Structure and Subcellular Localization of the Knob-Associated Histidine-Rich Protein of Plasmodium falciparum
Laura G. Pologe, Amalia Pavlovec, Helen Shio and Jeffrey V. Ravetch
Proceedings of the National Academy of Sciences of the United States of America
Vol. 84, No. 20 (Oct. 15, 1987), pp. 7139-7143
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/30373
Page Count: 5
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Plasmodium falciparum-infected erythrocytes bind to venular endothelial cells by means of electron-dense deformations (knobs) on the parasitized erythrocyte surface. The primary structure of a parasite-derived histidine-rich protein associated with the knob structure was deduced from cDNA sequence analysis. The 634 amino acid sequence is rich in lysine and histidine and contains three distinct, tandemly repeated domains. Indirect immunofluorescence, using affinity-purified monospecific antibodies directed against recombinant protein synthesized in Escherichia coli, localized the knob-associated histidine-rich protein to the membrane of knobby infected erythrocytes. Immunoelectron microscopy established that the protein is clustered on the cytoplasmic side of the erythrocyte membrane and is associated with the electron-dense knobs. A role for this histidine-rich protein in knob structure and cytoadherence is suggested based upon these data.
Proceedings of the National Academy of Sciences of the United States of America © 1987 National Academy of Sciences