Berman A, Shearing L N, Ng K F, Jinsart W, Foley M, Tilley L
Department of Biochemistry, La Trobe University, Bundoora, Victoria, Australia.
Mol Biochem Parasitol. 1994 Oct;67(2):235-43. doi: 10.1016/0166-6851(94)00136-7.
Erythrocytes infected with mature-stage malaria parasites accumulate phospholipids from exogenous sources. We show that the transport of N-(7-nitrobenzy-2-oxa-1,3-diazol-4-yl)-1,2- dipalmitoyl-sn-glycero-3-phosphatidylethanolamine (N-NBD-DPPE), from the erythrocyte membrane to the intracellular malaria parasite, is dependent upon metabolic energy. A photoreactive phospholipid analogue, N-[125I]iodo-4-azidosalicylamidyl-1, 2-dilauryl-sn-glycero-3-phosphatidylethanolamine (N-125I-ASA-DLPE), has been synthesised and used in an attempt to identify proteins involved in phospholipid trafficking in malaria-infected erythrocytes. This photoreactive probe was found to preferentially label a protein with an apparent molecular weight of 22 kDa. Photolabelling of the 22-kDa protein was enhanced upon ATP depletion of malaria-infected erythrocytes.
感染成熟阶段疟原虫的红细胞会从外源获取磷脂。我们发现,N-(7-硝基苯并-2-恶唑-1,3-二氮杂环丁烷-4-基)-1,2-二棕榈酰-sn-甘油-3-磷脂酰乙醇胺(N-NBD-DPPE)从红细胞膜转运至细胞内疟原虫的过程依赖于代谢能量。一种光反应性磷脂类似物,N-[¹²⁵I]碘-4-叠氮水杨酰胺基-1,2-二月桂酰-sn-甘油-3-磷脂酰乙醇胺(N-¹²⁵I-ASA-DLPE)已被合成,并用于尝试鉴定参与疟原虫感染红细胞中磷脂转运的蛋白质。发现这种光反应性探针优先标记一种表观分子量为22 kDa的蛋白质。在疟原虫感染的红细胞ATP耗竭时,22 kDa蛋白质的光标记增强。