免疫电镜
颗粒(地质)
细胞生物学
致密颗粒
恶性疟原虫
细胞器
生物
液泡
寄生虫寄主
超微结构
细胞质
抗体
免疫学
解剖
弓形虫
古生物学
疟疾
万维网
计算机科学
作者
Hideyuki Iriko,Tomoko Ishino,Hitoshi Otsuki,Daisuke Ito,Masashi Tachibana,Motomi Torii,Takafumi Tsuboi
标识
DOI:10.1016/j.parint.2018.06.001
摘要
Apical organellar proteins in Plasmodium falciparum merozoites play important roles upon invasion. To date, dense granule, the least studied apical organelle, secretes parasite proteins across the parasitophorous vacuole membrane (PVM) to remodel the infected erythrocyte. Although this phenomenon is key to parasite growth and virulence, only five proteins so far have been identified as dense granule proteins. Further elucidation of dense granule molecule(s) is therefore required. P. falciparum Exported Protein (EXP) 1, previously reported as a parasitophorous vacuole membrane (PVM) protein, is considered essential for parasite growth. In this study, we characterized EXP1 using specific anti-EXP1 antibodies generated by immunization of wheat germ cell-free produced recombinant EXP1. Immunofluorescence microscopy (IFA) demonstrated that EXP1 co-localized with RESA, indicating that the protein is initially localized to dense granules in merozoites, followed by translocation to the PVM. The EXP1 localization in dense granule of merozoites and its translocation to the PVM after invasion of erythrocytes were further confirmed by immunoelectron microscopy. Here, we demonstrate that EXP1 is one of the dense granule proteins in merozoites, which is then transported to the PVM after invasion.
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