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KAHRP dynamically relocalizes to remodeled actin junctions and associates with knob spirals in Plasmodium falciparum-infected erythrocytes
Molecular Microbiology ( IF 3.6 ) Pub Date : 2021-09-13 , DOI: 10.1111/mmi.14811
Cecilia P Sanchez 1 , Pintu Patra 2, 3 , Shih-Ying Scott Chang 4 , Christos Karathanasis 5 , Lukas Hanebutte 1 , Nicole Kilian 1 , Marek Cyrklaff 1 , Mike Heilemann 3, 5 , Ulrich S Schwarz 2, 3 , Mikhail Kudryashev 4 , Michael Lanzer 1
Affiliation  

The knob-associated histidine-rich protein (KAHRP) plays a pivotal role in the pathophysiology of Plasmodium falciparum malaria by forming membrane protrusions in infected erythrocytes, which anchor parasite-encoded adhesins to the membrane skeleton. The resulting sequestration of parasitized erythrocytes in the microvasculature leads to severe disease. Despite KAHRP being an important virulence factor, its physical location within the membrane skeleton is still debated, as is its function in knob formation. Here, we show by super-resolution microscopy that KAHRP initially associates with various skeletal components, including ankyrin bridges, but eventually colocalizes with remnant actin junctions. We further present a 35 Å map of the spiral scaffold underlying knobs and show that a KAHRP-targeting nanoprobe binds close to the spiral scaffold. Single-molecule localization microscopy detected ~60 KAHRP molecules/knob. We propose a dynamic model of KAHRP organization and a function of KAHRP in attaching other factors to the spiral scaffold.

中文翻译:

KAHRP 动态重新定位到重塑的肌动蛋白连接并与恶性疟原虫感染的红细胞中的旋钮螺旋相关联

旋钮相关富含组氨酸蛋白 (KAHRP) 在恶性疟原虫的病理生理学中起关键作用疟疾通过在受感染的红细胞中形成膜突起,将寄生虫编码的粘附素锚定在膜骨架上。由此产生的微血管系统中寄生的红细胞的隔离导致严重的疾病。尽管 KAHRP 是一个重要的毒力因子,但它在膜骨架内的物理位置仍然存在争议,它在结节形成中的功能也是如此。在这里,我们通过超分辨率显微镜显示,KAHRP 最初与各种骨骼成分相关联,包括锚蛋白桥,但最终与残余肌动蛋白连接共定位。我们进一步展示了旋钮下方螺旋支架的 35 Å 图,并显示 KAHRP 靶向纳米探针与螺旋支架结合。单分子定位显微镜检测到~60个KAHRP分子/旋钮。
更新日期:2021-09-13
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