Sam-Yellowe T Y, Fujioka H, Aikawa M, Hall T, Drazba J A
Cleveland State University, Department of Biological, Geological and Environmental Sciences, OH 44115, USA.
Parasitol Res. 2001 Mar;87(3):173-85. doi: 10.1007/pl00008572.
We report on the characterization of monoclonal antibodies against Plasmodium falciparum schizonts, which recognize parasite proteins of 130 kDa and 20 kDa. The 130-kDa protein was released by alkaline sodium carbonate treatment, suggesting that the protein is a peripheral membrane protein, while the 20-kDa protein remained associated with the membranes following alkali treatment, suggesting it may be an integral membrane protein. Both proteins were localized to large cytoplasmic vesicles within the cytoplasm of trophozoite and schizont-infected erythrocytes by immunofluorescence assay and confocal microscopy. Both proteins colocalized with Bodipy-ceramide in trophozoite and immature schizont-infected erythrocytes, but not in segmenters. The 130-kDa protein was localized by immunoelectron microscopy (IEM) to Maurer's clefts underneath knobs in a knobby and cytoadherent (K +/ C+) P. falciparum strain. No IEM reactivity was obtained in a knobless and non-cytoadherent (K-/C-)
我们报告了针对恶性疟原虫裂殖体的单克隆抗体的特性,这些抗体识别130 kDa和20 kDa的寄生虫蛋白。130 kDa的蛋白经碱性碳酸钠处理后释放,表明该蛋白是外周膜蛋白,而20 kDa的蛋白在碱处理后仍与膜结合,表明它可能是整合膜蛋白。通过免疫荧光测定和共聚焦显微镜检查,这两种蛋白均定位于滋养体和裂殖体感染红细胞细胞质内的大型细胞质囊泡中。在滋养体和未成熟裂殖体感染的红细胞中,这两种蛋白均与Bodipy-神经酰胺共定位,但在裂殖子中则不然。通过免疫电子显微镜(IEM),在一个有结节且细胞黏附性强(K +/ C+)的恶性疟原虫菌株中,130 kDa的蛋白定位于结节下方的毛氏小窝。在无结节且无细胞黏附性(K-/C-)的菌株中未获得IEM反应性。