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本文引用的文献

1
The molecular basis for perforin oligomerization and transmembrane pore assembly.穿孔素寡聚化和跨膜孔组装的分子基础。
Immunity. 2009 May;30(5):684-95. doi: 10.1016/j.immuni.2009.03.016. Epub 2009 May 14.
2
Apicomplexan parasites co-opt host calpains to facilitate their escape from infected cells.顶复门寄生虫利用宿主的钙蛋白酶来促进它们从被感染的细胞中逃脱。
Science. 2009 May 8;324(5928):794-7. doi: 10.1126/science.1171085. Epub 2009 Apr 2.
3
The interactomics of sortilin: an ancient lysosomal receptor evolving new functions.sortilin的相互作用组学:一种进化出新功能的古老溶酶体受体
Histol Histopathol. 2009 Apr;24(4):481-92. doi: 10.14670/HH-24.481.
4
Rapid membrane disruption by a perforin-like protein facilitates parasite exit from host cells.一种穿孔素样蛋白导致的快速膜破坏促进寄生虫从宿主细胞中逸出。
Science. 2009 Jan 23;323(5913):530-3. doi: 10.1126/science.1165740. Epub 2008 Dec 18.
5
PlasmoDB: a functional genomic database for malaria parasites.疟原虫功能基因组数据库(PlasmoDB)
Nucleic Acids Res. 2009 Jan;37(Database issue):D539-43. doi: 10.1093/nar/gkn814. Epub 2008 Oct 28.
6
The MACPF/CDC family of pore-forming toxins.成孔毒素的MACPF/CDC家族。
Cell Microbiol. 2008 Sep;10(9):1765-74. doi: 10.1111/j.1462-5822.2008.01191.x. Epub 2008 Jun 28.
7
Microneme proteins in apicomplexans.顶复门原虫中的微线体蛋白
Subcell Biochem. 2008;47:33-45. doi: 10.1007/978-0-387-78267-6_2.
8
Host cell traversal is important for progression of the malaria parasite through the dermis to the liver.宿主细胞穿越对于疟原虫通过真皮进入肝脏的进程很重要。
Cell Host Microbe. 2008 Feb 14;3(2):88-96. doi: 10.1016/j.chom.2007.12.007.
9
Interaction between the human immunodeficiency virus type 1 Gag matrix domain and phosphatidylinositol-(4,5)-bisphosphate is essential for efficient gag membrane binding.1型人类免疫缺陷病毒Gag基质结构域与磷脂酰肌醇-(4,5)-二磷酸之间的相互作用对于有效的gag膜结合至关重要。
J Virol. 2008 Mar;82(5):2405-17. doi: 10.1128/JVI.01614-07. Epub 2007 Dec 19.
10
Subcellular discharge of a serine protease mediates release of invasive malaria parasites from host erythrocytes.一种丝氨酸蛋白酶的亚细胞释放介导侵袭性疟原虫从宿主红细胞的释放。
Cell. 2007 Dec 14;131(6):1072-83. doi: 10.1016/j.cell.2007.10.049.

顶复门穿孔素样蛋白

Apicomplexan perforin-like proteins.

作者信息

Kafsack Björn F C, Carruthers Vern B

机构信息

Department of Microbiology and Immunology; University of Michigan; Ann Arbor, MI USA.

出版信息

Commun Integr Biol. 2010 Jan;3(1):18-23. doi: 10.4161/cib.3.1.9794.

DOI:10.4161/cib.3.1.9794
PMID:20539776
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2881234/
Abstract

Numerous perforin-like proteins are encoded in the genomes of apicomplexan parasites, where they are expressed in various life-cycle stages and play critical roles in pathogenesis and lifecycle progression. These ApiPLPs are characterized by the presence of a MACPF domain, responsible for pore-formation in target membranes in a number of systems, including many bacterial pathogens and effector cells of the immune response. ApiPLP MACPF domains maintain the critical structural elements but are often present in new and intriguing domain arrangements. Recent work in Toxoplasma and Plasmodium has shown that ApiPLPs are important for breaching membranes during parasite egress and cell traversal. Here we present an overview of this important protein family from a structural, functional and phylogenetic perspective across the Apicomplexa.

摘要

许多穿孔素样蛋白编码于顶复门寄生虫的基因组中,它们在不同的生命周期阶段表达,并在发病机制和生命周期进展中发挥关键作用。这些顶复门穿孔素样蛋白(ApiPLPs)的特征是存在一个膜攻击复合物/穿孔素(MACPF)结构域,该结构域在许多系统中负责在靶膜上形成孔道,包括许多细菌病原体和免疫反应的效应细胞。ApiPLP的MACPF结构域保留了关键的结构元件,但通常以新的、有趣的结构域排列形式存在。近期针对弓形虫和疟原虫的研究表明,ApiPLPs对于寄生虫逸出和穿越细胞过程中的膜破裂很重要。在此,我们从结构、功能和系统发育的角度,对整个顶复门中这一重要的蛋白家族进行概述。