An exported heat shock protein 40 associates with pathogenesis-related knobs in Plasmodium falciparum infected erythrocytes.
An exported heat shock protein 40 associates with pathogenesis-related knobs in Plasmodium falciparum infected erythrocytes.
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DOI：
10.1371/journal.pone.0044605
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发表时间：
2012
期刊：
影响因子：
3.7
通讯作者：
Tatu U
中科院分区：
文献类型：
--
作者：
Acharya P;Chaubey S;Grover M;Tatu U
细胞表面结构称为旋钮是一个最重要的发病机制相关的蛋白质复合物部署的疟疾寄生虫恶性疟原虫在受感染的红细胞表面。尽管它们与该疾病有关，但它们的结构、运输机制及其组装过程仍然知之甚少。在这项研究中，我们探讨了寄生虫编码的Hsp 40类伴侣蛋白，即PFB 0090 c/PF3D7_0201800（KAHsp 40）在感染红细胞中的蛋白运输的可能作用。我们发现编码PF3D7_0201800的基因与结组分KAHRP和PfEMP 3一起位于染色体簇中。与旋钮组件一样，KAHsp 40也显示出转运至红细胞隔室所需的PEXEL基序的存在。实际上，亚细胞分级分离和免疫荧光分析（IFA）显示KAHsp 40以阶段依赖性方式在红细胞胞质中输出，定位为红细胞外周中的点状斑点，与Maurer裂明显不同，其结构可能是令人联想到的旋钮。双IFA分析显示PF3D7_0201800与结的标记物（KAHRP、PfEMP 1和PfEMP 3）和PEXEL易位子的组分（Hsp 101、PTEX 150）共定位。免疫共沉淀法证实KAHsp 40与KAHRP、PfEMP 3和Hsp 101形成复合物。我们的研究结果表明，潜在的参与寄生虫编码的热休克蛋白40在陪伴旋钮组装在红细胞室。
Cell surface structures termed knobs are one of the most important pathogenesis related protein complexes deployed by the malaria parasite Plasmodium falciparum at the surface of the infected erythrocyte. Despite their relevance to the disease, their structure, mechanisms of traffic and their process of assembly remain poorly understood. In this study, we have explored the possible role of a parasite-encoded Hsp40 class of chaperone, namely PFB0090c/PF3D7_0201800 (KAHsp40) in protein trafficking in the infected erythrocyte. We found the gene coding for PF3D7_0201800 to be located in a chromosomal cluster together with knob components KAHRP and PfEMP3. Like the knob components, KAHsp40 too showed the presence of PEXEL motif required for transport to the erythrocyte compartment. Indeed, sub-cellular fractionation and immunofluorescence analysis (IFA) showed KAHsp40 to be exported in the erythrocyte cytoplasm in a stage dependent manner localizing as punctuate spots in the erythrocyte periphery, distinctly from Maurer’s cleft, in structures which could be the reminiscent of knobs. Double IFA analysis revealed co-localization of PF3D7_0201800 with the markers of knobs (KAHRP, PfEMP1 and PfEMP3) and components of the PEXEL translocon (Hsp101, PTEX150). KAHsp40 was also found to be in a complex with KAHRP, PfEMP3 and Hsp101 as confirmed by co-immunoprecipitation assay. Our results suggest potential involvement of a parasite encoded Hsp40 in chaperoning knob assembly in the erythrocyte compartment.
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影响因子：
64.8
作者：
de Koning-Ward, Tania F.;Gilson, Paul R.;Boddey, Justin A.;Rug, Melanie;Smith, Brian J.;Papenfuss, Anthony T.;Sanders, Paul R.;Lundie, Rachel J.;Maier, Alexander G.;Cowman, Alan F.;Crabb, Brendan S.
通讯作者：
Crabb, Brendan S.
DOI：
10.1074/jbc.m111.330779
发表时间：
2012-03-02
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Mayer C;Slater L;Erat MC;Konrat R;Vakonakis I
通讯作者：
Vakonakis I
影响因子：
5.3
作者：
Spycher, Cornelia;Rug, Melanie;Tilley, Leann
通讯作者：
Tilley, Leann
影响因子：
64.5
作者：
Maier AG;Rug M;O'Neill MT;Brown M;Chakravorty S;Szestak T;Chesson J;Wu Y;Hughes K;Coppel RL;Newbold C;Beeson JG;Craig A;Crabb BS;Cowman AF
通讯作者：
Cowman AF
DOI：
10.1073/pnas.86.7.2428
发表时间：
1989-04-01
影响因子：
11.1
作者：
BIGGS, BA;KEMP, DJ;BROWN, GV
通讯作者：
BROWN, GV