Access

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

If You Use a Screen Reader

This content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.

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
Stable URL: http://www.jstor.org/stable/30373
Page Count: 5
  • Read Online (Free)
  • Subscribe ($19.50)
  • Cite this Item
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Primary Structure and Subcellular Localization of the Knob-Associated Histidine-Rich Protein of Plasmodium falciparum
Preview not available

Abstract

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.

Page Thumbnails

  • Thumbnail: Page 
7139
    7139
  • Thumbnail: Page 
7140
    7140
  • Thumbnail: Page 
7141
    7141
  • Thumbnail: Page 
7142
    7142
  • Thumbnail: Page 
7143
    7143