Zeitschrift für Parasitenkunde

, Volume 71, Issue 1, pp 41–51 | Cite as

The relationship to knobs of the 92,000 D protein specific for knobby strains ofPlasmodium falciparum

  • Jean-Paul Vernot-Hernandez
  • Hans-G. Heidrich
Original Investigations


A 92,000 D protein was identified associated with the membrane of host erythrocytes infected with the FCB1Plasmodium falciparum strain from Colombia. The same protein was identified in the knob-forming Gambian (and the Malayan Camp) strain, but was not present in all the corresponding knobless strains. In the FCB1 strain as well as in the FCR3 strain the protein is synthesized during the ring-stage period. The cleavage products of the 92,000 D protein were investigated by peptide mapping following limited proteolytic digestion withStaphylococcus aureus V8 protease. The 92,000 D protein cleavage products from both the Colombian and the Gambian strains were identical. Moreover, both the proteins were sensitive to trypsin and chymotrypsin and also to treatment with neuraminidase. Enzymatic removal of the protein from the erythrocyte membrane by trypsin or chymotrypsin did not affect parasite maturation. The merozoites thus produced were fully invasive and the morphology of the knobs was unaltered. When the erythrocyte membrane was treated with trypsin before the time of synthesis of the 92,000 D protein, it was not possible to identify the protein in membranes of later stages of infected erythrocytes, indicating that the protein cannot be inserted into the membrane cytoskeleton compartment. Knobs, however, were formed more or less normally, suggesting that it is not the accumulation of this protein which produces the knobs.


Trypsin Erythrocyte Membrane Chymotrypsin Cleavage Product Peptide Mapping 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer-Verlag 1985

Authors and Affiliations

  • Jean-Paul Vernot-Hernandez
    • 1
  • Hans-G. Heidrich
    • 1
  1. 1.Max-Planck-Institut für BiochemieMartinsried bei MünchenFederal Republic of Germany

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