Primary structure and subcellular localization of the knob-associated histidine-rich protein of Plasmodium falciparum Journal Article


Authors: Pologe, L. G.; Pavlovec, A.; Shio, H.; Ravetch, J. V.
Article Title: Primary structure and subcellular localization of the knob-associated histidine-rich protein of Plasmodium falciparum
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.
Keywords: genetics; molecular genetics; animal; animals; peptide; immunology; dna; amino acid sequence; molecular sequence data; nucleotide sequence; recombinant proteins; recombinant protein; peptides; base sequence; erythrocyte; plasmodium falciparum; erythrocytes; protozoan proteins; parasitology; erythrocyte membrane; article; protozoal protein; knob protein, plasmodium falciparum
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 84
Issue: 20
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 1987-10-01
Start Page: 7139
End Page: 7143
Language: English
DOI: 10.1073/pnas.84.20.7139
PUBMED: 3313387
PROVIDER: scopus
PMCID: PMC299245
DOI/URL:
Notes: Article -- Export Date: 5 February 2021 -- Source: Scopus
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  1. Jeffrey V. Ravetch
    72 Ravetch