Murray M C, Perkins M E
Laboratory of Biochemical Parasitology, Rockefeller University, New York, NY 10021.
Mol Biochem Parasitol. 1989 May 15;34(3):229-36. doi: 10.1016/0166-6851(89)90051-0.
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.
研究了恶性疟原虫感染导致的红细胞膜和细胞骨架蛋白的磷酸化变化。血影蛋白、带3蛋白、带4.1蛋白、锚蛋白和血型糖蛋白在正常红细胞中会发生磷酸化。由于疟原虫的裂殖子（寄生虫的细胞外阶段）侵入32P预标记的正常红细胞，所有主要的32P标记红细胞蛋白都会发生去磷酸化。随着寄生虫在细胞内从未成熟环状体阶段发育到成熟裂殖体阶段，可以观察到某些宿主蛋白（血影蛋白、锚蛋白和带3蛋白）的选择性磷酸化。在寄生虫发育的任何阶段，带4.1蛋白似乎都不会掺入[32P]磷酸盐。这些观察到的磷酸化变化可能对恶性疟原虫感染细胞中细胞骨架组织的调节很重要。
