title: Plasmodium falciparum double C2 domain protein, PfDOC2, binds to calcium when associated with membranes.
abstract: 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.
authors.affiliation: Department of Biology, Virginia Commonwealth University, Richmond, VA 23284-2012, United States.
authors.forename: Sophonie
authors.initials: S
authors.lastname: Jean
authors.affiliation: Department of Biology, Virginia Commonwealth University, Richmond, VA 23284-2012, United States.
authors.forename: Mónica A
authors.initials: MA
authors.lastname: Zapata-Jenks
authors.affiliation: Department of Biology, Virginia Commonwealth University, Richmond, VA 23284-2012, United States.
authors.forename: Julie M
authors.initials: JM
authors.lastname: Farley
authors.affiliation: Department of Forensic Science, Virginia Commonwealth University, Richmond, VA 23284-2012, United States.
authors.forename: Erin
authors.initials: E
authors.lastname: Tracy
authors.affiliation: Department of Biology, Manhattan College, Riverdale, NY 10471, United States. Electronic address: ghislaine.mayer@manhattan.edu.
authors.forename: D C Ghislaine
authors.initials: DC
authors.lastname: Mayer
mesh_terms: D000818:Animals; D002118:Calcium / Q000378:metabolism*; D002135:Calcium-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D003001:Cloning, Molecular; D005455:Fluorescent Antibody Technique; D005786:Gene Expression Regulation; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D010963:Plasmodium falciparum / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011493:Protein Kinase C / Q000235:genetics / Q000378:metabolism*; D015800:Protozoan Proteins / Q000235:genetics / Q000378:metabolism*; D011817:Rabbits; D051381:Rats
chemical_list: D002135:Calcium-Binding Proteins; D008565:Membrane Proteins; D015800:Protozoan Proteins; D011493:Protein Kinase C; D002118:Calcium
keywords: Calcium lipid-binding; DOC2; Double C2 domain; Malaria; Plasmodium