Plasmodium falciparum induces reorganization of host membrane proteins during intraerythrocytic growth.
The virulence of the malaria parasite, Plasmodium falciparum, is due in large part to the way in which it modifies the membrane of its erythrocyte host. In this work we have used confocal microscopy and fluorescence recovery after photo-bleaching to examine the lateral mobility of host membrane proteins in erythrocytes infected with P falciparum at different stages of parasite growth. The erythrocyte membrane proteins band 3 and glycophorin show a marked decrease in mobility during the trophozoite stage of growth. Erythrocytes infected with a parasite strain that does not express the knob-associated histidine-rich protein show similar effects, indicating that this parasite protein does not contribute to the immobilization of the host proteins. Erythrocytes infected with ring-stage parasites exhibit intermediate mobility indicating that the parasite is able to modify its host prior to its active feeding stage.
Parker
Phillip D
PD
Department of Biochemist and the Cooperative Center for Diagnostics, La Trobe University, Victoria 3086, Australia.
Tilley
Leann
L
Klonis
Nectarios
N
D000818:Animals; D001457:Anion Exchange Protein 1, Erythrocyte / Q000378:metabolism; D004910:Erythrocyte Membrane / Q000378:metabolism / Q000469:parasitology*; D036681:Fluorescence Recovery After Photobleaching; D006021:Glycophorins / Q000378:metabolism; D006790:Host-Parasite Interactions; D006801:Humans; D016778:Malaria, Falciparum / Q000378:metabolism / Q000469:parasitology*; D008560:Membrane Fluidity / Q000502:physiology; D010963:Plasmodium falciparum / Q000254:growth & development* / Q000502:physiology*
D001457:Anion Exchange Protein 1, Erythrocyte; D006021:Glycophorins