Phosphorylation of erythrocyte membrane and cytoskeleton proteins in cells infected with Plasmodium falciparum.
Phosphorylation changes in the erythrocyte membrane and cytoskeletal proteins as a consequence of infection by the malarial parasite Plasmodium falciparum were examined. Spectrin, band 3, band 4.1, ankyrin and glycophorin are phosphorylated in normal erythrocytes. As a consequence of invasion by the merozoite, the extracellular stage of the parasite, into 32P-prelabeled normal erythrocytes, all the major 32P-labeled erythrocyte proteins are dephosphorylated. As the parasite develops intracellularly from the immature ring stage to the mature schizont stage, selective phosphorylation of certain host proteins, spectrin, ankyrin and band 3 is observed. Band 4.1 does not appear to incorporate [32P]phosphate at any stage of parasite development. These observed phosphorylation changes may be important in the regulation of the cytoskeletal organization in P. falciparum-infected cells.
Murray
M C
MC
Laboratory of Biochemical Parasitology, Rockefeller University, New York, NY 10021.
Perkins
M E
ME
D000818:Animals; D017487:Ankyrins; D001798:Blood Proteins / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism / Q000469:parasitology* / Q000648:ultrastructure; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism*; D010766:Phosphorylation; D010963:Plasmodium falciparum / Q000378:metabolism* / Q000502:physiology; D011233:Precipitin Tests; D013049:Spectrin / Q000378:metabolism
D017487:Ankyrins; D001798:Blood Proteins; D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; D013049:Spectrin