Electron microscope cytochemistry of host-parasite membrane interactions in malaria.
Two membrane-bound enzymes were localized by electron microscope cytochemical techniques in Plasmodium lophurae and its host erythrocyte. Parasites were prepared by saponin lysis, French pressure cell lysis, or anti-red blood cell serum lysis; infected and uninfected erythrocyte ghosts were prepared by saponin or French pressure cell lysis. Enzyme incubations were performed on unfixed cells. Adenosinetriphosphatase (EC 3.6.1.3) activity was found on the inside of the ghost membrane and on the inside of the outer parasite membrane. NADH oxidase was found on the outside of the erythrocyte membrane and on the outside of the parasite outer membrane. The parasite plasma membrane was negative for both enzymes. The location of both enzymes on the outer parasite membrane were reversed from what one would have expected if the outer membrane had remained merely an invaginated erythrocyte membrane. It is concluded that the outer membrane, although derived from the red cell membrane, has been altered by its association with the malarial parasite.
D000251:Adenosine Triphosphatases / Q000032:analysis; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D004372:Ducks; D004912:Erythrocytes / Q000201:enzymology / Q000469:parasitology*; D008288:Malaria / Q000469:parasitology*; D009247:NADH, NADPH Oxidoreductases / Q000032:analysis; D010961:Plasmodium / Q000201:enzymology*
D009247:NADH, NADPH Oxidoreductases; D000251:Adenosine Triphosphatases