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Exp Parasitol. 2014 Sep;144:91-5. doi: 10.1016/j.exppara.2014.06.015. Epub 2014 Jun 30.

Plasmodium falciparum double C2 domain protein, PfDOC2, binds to calcium when associated with membranes.

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  • 1Department of Biology, Virginia Commonwealth University, Richmond, VA 23284-2012, United States.
  • 2Department of Forensic Science, Virginia Commonwealth University, Richmond, VA 23284-2012, United States.
  • 3Department of Biology, Manhattan College, Riverdale, NY 10471, United States. Electronic address: ghislaine.mayer@manhattan.edu.


The pathogenesis of malaria is strongly correlated with secretion of the micronemes, the apical organelles which contain the adhesins required for invasion of Plasmodium falciparum into human erythrocytes. A critical event in P. falciparum erythrocyte invasion is the production of calcium transients. After entering the cell, Ca(2+) binds to soluble Ca(2+)-binding proteins, such as the double C2 domains (DOC2). Recently, deletion of a P. falciparum DOC2 protein, PfDOC2, was shown to cause impairment in microneme secretion. However, PfDOC2 remains poorly characterized. Here, we report that PfDOC2 is expressed throughout the erythrocytic cycle and demonstrate that it is associated with membrane fractions and binds to calcium when it is part of these membranous structures. In summary, we show that PfDOC2 is a calcium lipid-binding protein of the protein kinase C type of DOC2 proteins.

Copyright © 2014 Elsevier Inc. All rights reserved.


Calcium lipid-binding; DOC2; Double C2 domain; Malaria; Plasmodium

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