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疟疾寄生虫分拣站的分子参与者。

Molecular Players at the Sorting Stations of Malaria Parasite .

机构信息

Department of Biochemistry, Govt. College for Girls, Ludhiana, Punjab, India (Affiliated to Panjab University, Chandigarh), India.

Department of Biotechnology, Guru Nanak Dev University Amritsar, Punjab, India.

出版信息

Curr Protein Pept Sci. 2024;25(6):427-437. doi: 10.2174/0113892037282522240130090156.

DOI:10.2174/0113892037282522240130090156
PMID:38409726
Abstract

The apicomplexan pathogenic parasite ' (Pf) is responsible for most of the malaria related mortality. It resides in and refurbishes the infected red blood cells (iRBCs) for its own survival and to suffice its metabolic needs. Remodeling of host erythrocytes involves alteration of physical and biochemical properties of the membrane and genesis of new parasite induced structures within the iRBCs. The generated structures include knobs and solute ion channels on the erythrocyte surface and specialized organelles i.e. Maurer's clefts (MCs) in the iRBC cytosol. The above processes are mediated by exporting a large repertoire of proteins to the host cell, most of which are transported MCs, the sorting stations in parasitized erythrocytes. Information about MC biogenesis and the molecules involved in maintaining MC architecture remains incompletely elucidated. Here, we have compiled a list of experimentally known MC resident proteins, several of which have roles in maintaining its architecture and function. Our short review covers available data on the domain organization, orthologues, topology and specific roles of these proteins. We highlight the current knowledge gaps in our understanding of MCs as crucial organelles involved in parasite biology and disease pathogenesis.

摘要

疟原虫寄生虫是引起疟疾的主要病原体,它寄生在感染的红细胞(iRBC)中,并对其进行修复,以维持自身的生存和满足代谢需求。宿主红细胞的重塑涉及到膜的物理和生化性质的改变,以及在 iRBC 中产生新的寄生虫诱导结构。生成的结构包括红细胞表面的小结和溶质离子通道,以及 iRBC 细胞质中的特殊细胞器即 Maurer 氏裂隙(MCs)。这些过程是通过向宿主细胞输出大量蛋白质来介导的,其中大多数蛋白质被运输到 MCs,即寄生虫化红细胞中的分拣站。关于 MC 发生和维持 MC 结构的分子的信息仍然不完全清楚。在这里,我们编译了一份实验已知的 MC 驻留蛋白列表,其中有几个在维持其结构和功能方面发挥作用。我们的简短综述涵盖了这些蛋白质的结构域组织、同源物、拓扑结构和特定功能的现有数据。我们强调了我们对 MC 作为涉及寄生虫生物学和疾病发病机制的关键细胞器的理解中的当前知识空白。

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本文引用的文献

1
Exported J domain proteins of the human malaria parasite.人类疟原虫的输出型J结构域蛋白
Front Mol Biosci. 2022 Aug 31;9:978663. doi: 10.3389/fmolb.2022.978663. eCollection 2022.
2
Deletion of the Plasmodium falciparum exported protein PTP7 leads to Maurer's clefts vesiculation, host cell remodeling defects, and loss of surface presentation of EMP1.缺失疟原虫分泌蛋白 PTP7 导致 Maurer 氏袢泡化、宿主细胞重塑缺陷以及 EMP1 表面呈现丢失。
PLoS Pathog. 2022 Aug 5;18(8):e1009882. doi: 10.1371/journal.ppat.1009882. eCollection 2022 Aug.
3
Trafficking and Association of MC-2TM with the Maurer's Clefts.
疟原虫多蛋白转运器2(MC-2TM)与疟原虫毛氏小管的转运及关联
Pathogens. 2021 Apr 5;10(4):431. doi: 10.3390/pathogens10040431.
4
Role of Plasmodium falciparum Protein GEXP07 in Maurer's Cleft Morphology, Knob Architecture, and P. falciparum EMP1 Trafficking.恶性疟原虫蛋白 GEXP07 在马尔氏裂殖体形态、空泡结构和疟原虫 EMP1 转运中的作用。
mBio. 2020 Mar 17;11(2):e03320-19. doi: 10.1128/mBio.03320-19.
5
Plasmodium helical interspersed subtelomeric family-an enigmatic piece of the Plasmodium biology puzzle.疟原虫螺旋交错端粒家族——疟原虫生物学之谜中的一个神秘片段。
Parasitol Res. 2019 Oct;118(10):2753-2766. doi: 10.1007/s00436-019-06420-9. Epub 2019 Aug 15.
6
CX3CL1 binding protein-2 (CBP2) of Plasmodium falciparum binds nucleic acids.疟原虫 CX3CL1 结合蛋白-2(CBP2)与核酸结合。
Int J Biol Macromol. 2019 Oct 1;138:996-1005. doi: 10.1016/j.ijbiomac.2019.07.178. Epub 2019 Jul 26.
7
Plasmodium falciparum protein 'PfJ23' hosts distinct binding sites for major virulence factor 'PfEMP1' and Maurer's cleft marker 'PfSBP1'.恶性疟原虫蛋白 'PfJ23' 拥有独特的结合位点,可分别与主要毒力因子 'PfEMP1' 和 Maurer 裂殖环标记 'PfSBP1' 结合。
Pathog Dis. 2018 Dec 1;76(9):5255127. doi: 10.1093/femspd/fty090.
8
PHISTc protein family members localize to different subcellular organelles and bind Plasmodium falciparum major virulence factor PfEMP-1.PHISTc 蛋白家族成员定位于不同的亚细胞细胞器,并与恶性疟原虫主要毒力因子 PfEMP-1 结合。
FEBS J. 2018 Jan;285(2):294-312. doi: 10.1111/febs.14340. Epub 2017 Dec 10.
9
Plasmodium falciparum exported protein PFE60 influences Maurer's clefts architecture and virulence complex composition.恶性疟原虫输出蛋白 PFE60 影响 Maurer 氏裂隙结构和毒力复合物组成。
Int J Parasitol. 2018 Jan;48(1):83-95. doi: 10.1016/j.ijpara.2017.09.003. Epub 2017 Nov 1.
10
Proteomic analysis of exported chaperone/co-chaperone complexes of P. falciparum reveals an array of complex protein-protein interactions.疟原虫分泌伴侣/共伴侣复合物的蛋白质组学分析揭示了一系列复杂的蛋白质-蛋白质相互作用。
Sci Rep. 2017 Feb 20;7:42188. doi: 10.1038/srep42188.