Preferential binding of Plasmodium falciparum SERA and rhoptry proteins to erythrocyte membrane inner leaflet phospholipids.
Proteins of an apical organelle, the rhoptry, of Plasmodium falciparum are secreted into the host erythrocyte membrane during merozoite invasion. To identify the membrane-binding site for rhoptry proteins, we examined the binding of parasite proteins to phospholipid vesicles. A specific interaction between the rhoptry proteins of 140, 130, and 110 kDa to vesicles containing phosphatidylserine and phosphatidylinositol was observed. Both phospholipids are preferentially localized on the inner leaflet of the bilayer. Binding to other phospholipids, including sphingomyelin, was considerably less. In addition, the 120-kDa serine repeat antigen known as SERA, which was determined to be present on the merozoite, bound to phosphatidylserine vesicles and much less to vesicles of other phospholipids. Both the rhoptry and SERA proteins exhibited a preference for phosphatidylserine with short acyl side chains. Specific binding of SERA and the rhoptry proteins to phospholipids of the inner leaflet of membranes suggests a possible mechanism by which the protein facilitate invasion into host cells.
Perkins
M E
ME
Laboratory of Biochemical Parasitology, Rockefeller University, New York, New York 10023.
Ziefer
A
A
D000818:Animals; D000953:Antigens, Protozoan / Q000032:analysis / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D006801:Humans; D010743:Phospholipids / Q000378:metabolism*; D010963:Plasmodium falciparum / Q000276:immunology*; D015800:Protozoan Proteins / Q000378:metabolism*
D000953:Antigens, Protozoan; D010743:Phospholipids; D015800:Protozoan Proteins; C057495:serine repeat antigen, Plasmodium