Hijacking of the Host Ubiquitin Network by Legionella pneumophila
Protein ubiquitination is critical for regulation of numerous eukaryotic cellular processes such as protein homeostasis, cell cycle progression, immune response, DNA repair, and vesicular trafficking. Ubiquitination often leads to the alteration of protein stability, subcellular localization, or int...
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doaj-605a875adfc342f3975ddad9a099920c2020-11-24T23:51:54ZengFrontiers Media S.A.Frontiers in Cellular and Infection Microbiology2235-29882017-12-01710.3389/fcimb.2017.00487304328Hijacking of the Host Ubiquitin Network by Legionella pneumophilaJiazhang Qiu0Jiazhang Qiu1Zhao-Qing Luo2Zhao-Qing Luo3Zhao-Qing Luo4Center of Infection and Immunity, First Hospital, Jilin University, Changchun, ChinaKey Laboratory of Zoonosis, Ministry of Education, College of Veterinary Medicine, Jilin University, Changchun, ChinaCenter of Infection and Immunity, First Hospital, Jilin University, Changchun, ChinaKey Laboratory of Zoonosis, Ministry of Education, College of Veterinary Medicine, Jilin University, Changchun, ChinaDepartment of Biological Sciences, Purdue Institute for Inflammation, Immunology and Infectious Diseases, Purdue University, West Lafayette, IN, United StatesProtein ubiquitination is critical for regulation of numerous eukaryotic cellular processes such as protein homeostasis, cell cycle progression, immune response, DNA repair, and vesicular trafficking. Ubiquitination often leads to the alteration of protein stability, subcellular localization, or interaction with other proteins. Given the importance of ubiquitination in the regulation of host immunity, it is not surprising that many infectious agents have evolved strategies to interfere with the ubiquitination network with sophisticated mechanisms such as functional mimicry. The facultative intracellular pathogen Legionella pneumophila is the causative agent of Legionnaires' disease. L. pneumophila is phagocytosed by macrophages and is able to replicate within a niche called Legionella-containing vacuole (LCV). The biogenesis of LCV is dependent upon the Dot/Icm type IV secretion system which delivers more than 330 effector proteins into host cytosol. The optimal intracellular replication of L. pneumophila requires the host ubiquitin-proteasome system. Furthermore, membranes of the bacterial phagosome are enriched with ubiquitinated proteins in a way that requires its Dot/Icm type IV secretion system, suggesting the involvement of effectors in the manipulation of the host ubiquitination machinery. Here we summarize recent advances in our understanding of mechanisms exploited by L. pneumophila effector proteins to hijack the host ubiquitination pathway.http://journal.frontiersin.org/article/10.3389/fcimb.2017.00487/fulltype IV secretioneffectorsposttranslational modificationbacterial virulencecell signaling |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Jiazhang Qiu Jiazhang Qiu Zhao-Qing Luo Zhao-Qing Luo Zhao-Qing Luo |
spellingShingle |
Jiazhang Qiu Jiazhang Qiu Zhao-Qing Luo Zhao-Qing Luo Zhao-Qing Luo Hijacking of the Host Ubiquitin Network by Legionella pneumophila Frontiers in Cellular and Infection Microbiology type IV secretion effectors posttranslational modification bacterial virulence cell signaling |
author_facet |
Jiazhang Qiu Jiazhang Qiu Zhao-Qing Luo Zhao-Qing Luo Zhao-Qing Luo |
author_sort |
Jiazhang Qiu |
title |
Hijacking of the Host Ubiquitin Network by Legionella pneumophila |
title_short |
Hijacking of the Host Ubiquitin Network by Legionella pneumophila |
title_full |
Hijacking of the Host Ubiquitin Network by Legionella pneumophila |
title_fullStr |
Hijacking of the Host Ubiquitin Network by Legionella pneumophila |
title_full_unstemmed |
Hijacking of the Host Ubiquitin Network by Legionella pneumophila |
title_sort |
hijacking of the host ubiquitin network by legionella pneumophila |
publisher |
Frontiers Media S.A. |
series |
Frontiers in Cellular and Infection Microbiology |
issn |
2235-2988 |
publishDate |
2017-12-01 |
description |
Protein ubiquitination is critical for regulation of numerous eukaryotic cellular processes such as protein homeostasis, cell cycle progression, immune response, DNA repair, and vesicular trafficking. Ubiquitination often leads to the alteration of protein stability, subcellular localization, or interaction with other proteins. Given the importance of ubiquitination in the regulation of host immunity, it is not surprising that many infectious agents have evolved strategies to interfere with the ubiquitination network with sophisticated mechanisms such as functional mimicry. The facultative intracellular pathogen Legionella pneumophila is the causative agent of Legionnaires' disease. L. pneumophila is phagocytosed by macrophages and is able to replicate within a niche called Legionella-containing vacuole (LCV). The biogenesis of LCV is dependent upon the Dot/Icm type IV secretion system which delivers more than 330 effector proteins into host cytosol. The optimal intracellular replication of L. pneumophila requires the host ubiquitin-proteasome system. Furthermore, membranes of the bacterial phagosome are enriched with ubiquitinated proteins in a way that requires its Dot/Icm type IV secretion system, suggesting the involvement of effectors in the manipulation of the host ubiquitination machinery. Here we summarize recent advances in our understanding of mechanisms exploited by L. pneumophila effector proteins to hijack the host ubiquitination pathway. |
topic |
type IV secretion effectors posttranslational modification bacterial virulence cell signaling |
url |
http://journal.frontiersin.org/article/10.3389/fcimb.2017.00487/full |
work_keys_str_mv |
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