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嗜肺军团菌调节宿主泛素化途径的效应因子及其分子机制研究进展

Effector and molecular mechanism of Legionella pneumophila regulating host ubiquitination pathway: a review
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摘要 嗜肺军团菌是一种胞内寄生菌,其通过特有的Dot/Icm Type-IVB分泌系统向胞浆内分泌大量效应因子,其中已知参与宿主泛素化调控的效应因子有十多种。这些效应因子通过对宿主泛素化途径进行调控来达到逃避宿主免疫系统"监视"并大量增殖的目的。参与调控宿主泛素化途径的效应因子包括AnkB、SidC、LubX、SidH、LegU1、GobX、RavD、DupA、DupB、SidJ、Ceg23、MvcA、MavC及SidE家族蛋白等。随着对嗜肺军团菌效应因子功能及结构研究的深入,它们的作用机制逐渐被揭示。本文对其中几种重要嗜肺军团菌效应因子的生物学结构和分子机制进行系统总结,有利于综合了解嗜肺军团菌参与调控宿主泛素化系统的复杂过程。 Legionella pneumophila secretes a large number of effectors into the cytoplasm through its unique Dot/Icm type-IVB secretion system, among which there are more than ten effectors known to participate in regulation of host ubiquitination. These effectors achieve the purpose of evading surveillance by the host immune system and proliferation by regulating the host ubiquitination pathway. The effectors involved in regulating the host ubiquitination pathway include AnkB, SidC, LubX, SidH, LegU1, GobX, RavD, DupA, DupB, SidJ, Ceg23, MvcA, MavC and SidE family proteins. Through the gradually in-depth study of the functional experiments and structural biology of these effect factors, their relatively complete molecular mechanism has gradually been revealed. This article reviews several important L. pneumophila effectors and their biological structure and molecular mechanism, which is helpful to comprehensively understand the complex process of Legionella pneumophila involved in regulating the host ubiquitination system.
作者 黄旖旎 关洪鑫 欧阳松应 HUANG Yini;GUAN Hongxin;OUYANG Songying(College of Life Sciences,Fujian Normal University,Fuzhou,Fujian 350117,China;Fujian Normal University,Biomedical Research Center of South China,Fuzhou,Fujian 350117,China)
出处 《微生物学通报》 CAS CSCD 北大核心 2021年第6期2155-2169,共15页 Microbiology China
基金 国家自然科学基金(31770948,31570875) 福建省海洋经济发展补助项目(FJHJF-L-2020-2)。
关键词 嗜肺军团菌 效应因子 泛素化 生物学结构 分子机制 Legionella pneumophila effector ubiquitination biological structure molecular mechanism
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  • 1秘彩莉,刘旭,张学勇.F-box蛋白质在植物生长发育中的功能[J].遗传,2006,28(10):1337-1342. 被引量:41
  • 2Schwartz D C, Hochstrasser M. A superfamily of protein tags: ubiquitin, SUMO and related modifiers. Trends Biochem Sci, 2003, 28: 321-328.
  • 3Herrmann J, Lerman L O, Lerman A. Ubiquitin and ubiquitin-like proteins in protein regulation. Circ Res, 2007, 100:1276-1291.
  • 4Muratani M, Tansey W P. How the ubiquitin-proteasome system controls transcription. Nat Rev Mol Cell Biol, 2003, 4:192-201.
  • 5Shaid S, Brandts C H, Serve H, et al. Ubiquitination and selective antophagy. Cell Death Differ, 2013, 20:21-30.
  • 6Ulrich H D, Walden H. Ubiquitin signalling in DNA replication and repair. Nat Rev Mol Cell Biol, 2010, 11:479-489.
  • 7Vucic D, Dixit V M, Wertz I E. Ubiquitylation in apoptosis: a post-translational modification at the edge of life and death. Nat Rev Mol Cell Biol, 2011, 12:439-452.
  • 8Haglund K, Dikic I. The role of ubiquitylation in receptor endocytosis and endosomal sorting. J Cell Sci, 2012, 125:265-275.
  • 9Goldstein G, Scheid M, Hammerling U, et al. Isolation of a polypeptide that has lymphocyte-differentiating properties and is probably represented universally in living cells. Proc Natl Acad Sci USA, 1975, 72:11-15.
  • 10Deshaies R J, Joazeiro C A. Ring domain E3 ubiquitin ligases. Annu Rev Biochem, 2009, 78:399-434.

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