The Ubiquitination System within Bacterial Host–Pathogen Interactions
Ubiquitination of proteins, like phosphorylation and acetylation, is an important regulatory aspect influencing numerous and various cell processes, such as immune response signaling and autophagy. The study of ubiquitination has become essential to learning about host–pathogen interactions, and a b...
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MDPI AG
2021-03-01
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Online Access: | https://www.mdpi.com/2076-2607/9/3/638 |
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author | Vera Vozandychova Pavla Stojkova Kamil Hercik Pavel Rehulka Jiri Stulik |
author_facet | Vera Vozandychova Pavla Stojkova Kamil Hercik Pavel Rehulka Jiri Stulik |
author_sort | Vera Vozandychova |
collection | DOAJ |
description | Ubiquitination of proteins, like phosphorylation and acetylation, is an important regulatory aspect influencing numerous and various cell processes, such as immune response signaling and autophagy. The study of ubiquitination has become essential to learning about host–pathogen interactions, and a better understanding of the detailed mechanisms through which pathogens affect ubiquitination processes in host cell will contribute to vaccine development and effective treatment of diseases. Pathogenic bacteria (e.g., <i>Salmonella enterica</i>, <i>Legionella pneumophila</i> and <i>Shigella flexneri</i>) encode many effector proteins, such as deubiquitinating enzymes (DUBs), targeting the host ubiquitin machinery and thus disrupting pertinent ubiquitin-dependent anti-bacterial response. We focus here upon the host ubiquitination system as an integral unit, its interconnection with the regulation of inflammation and autophagy, and primarily while examining pathogens manipulating the host ubiquitination system. Many bacterial effector proteins have already been described as being translocated into the host cell, where they directly regulate host defense processes. Due to their importance in pathogenic bacteria progression within the host, they are regarded as virulence factors essential for bacterial evasion. However, in some cases (e.g., <i>Francisella tularensis</i>) the host ubiquitination system is influenced by bacterial infection, although the responsible bacterial effectors are still unknown. |
first_indexed | 2024-03-10T13:05:27Z |
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institution | Directory Open Access Journal |
issn | 2076-2607 |
language | English |
last_indexed | 2024-03-10T13:05:27Z |
publishDate | 2021-03-01 |
publisher | MDPI AG |
record_format | Article |
series | Microorganisms |
spelling | doaj.art-1004071f3d264bad817254f5c1f914852023-11-21T11:07:52ZengMDPI AGMicroorganisms2076-26072021-03-019363810.3390/microorganisms9030638The Ubiquitination System within Bacterial Host–Pathogen InteractionsVera Vozandychova0Pavla Stojkova1Kamil Hercik2Pavel Rehulka3Jiri Stulik4Department of Molecular Pathology and Biology, Faculty of Military Health Sciences, University of Defence, Trebesska 1575, 50001 Hradec Kralove, Czech RepublicDepartment of Molecular Pathology and Biology, Faculty of Military Health Sciences, University of Defence, Trebesska 1575, 50001 Hradec Kralove, Czech RepublicDepartment of Molecular Pathology and Biology, Faculty of Military Health Sciences, University of Defence, Trebesska 1575, 50001 Hradec Kralove, Czech RepublicDepartment of Molecular Pathology and Biology, Faculty of Military Health Sciences, University of Defence, Trebesska 1575, 50001 Hradec Kralove, Czech RepublicDepartment of Molecular Pathology and Biology, Faculty of Military Health Sciences, University of Defence, Trebesska 1575, 50001 Hradec Kralove, Czech RepublicUbiquitination of proteins, like phosphorylation and acetylation, is an important regulatory aspect influencing numerous and various cell processes, such as immune response signaling and autophagy. The study of ubiquitination has become essential to learning about host–pathogen interactions, and a better understanding of the detailed mechanisms through which pathogens affect ubiquitination processes in host cell will contribute to vaccine development and effective treatment of diseases. Pathogenic bacteria (e.g., <i>Salmonella enterica</i>, <i>Legionella pneumophila</i> and <i>Shigella flexneri</i>) encode many effector proteins, such as deubiquitinating enzymes (DUBs), targeting the host ubiquitin machinery and thus disrupting pertinent ubiquitin-dependent anti-bacterial response. We focus here upon the host ubiquitination system as an integral unit, its interconnection with the regulation of inflammation and autophagy, and primarily while examining pathogens manipulating the host ubiquitination system. Many bacterial effector proteins have already been described as being translocated into the host cell, where they directly regulate host defense processes. Due to their importance in pathogenic bacteria progression within the host, they are regarded as virulence factors essential for bacterial evasion. However, in some cases (e.g., <i>Francisella tularensis</i>) the host ubiquitination system is influenced by bacterial infection, although the responsible bacterial effectors are still unknown.https://www.mdpi.com/2076-2607/9/3/638ubiquitinationdeubiquitinating enzymes (DUBs)effector proteinhost–pathogen interaction |
spellingShingle | Vera Vozandychova Pavla Stojkova Kamil Hercik Pavel Rehulka Jiri Stulik The Ubiquitination System within Bacterial Host–Pathogen Interactions Microorganisms ubiquitination deubiquitinating enzymes (DUBs) effector protein host–pathogen interaction |
title | The Ubiquitination System within Bacterial Host–Pathogen Interactions |
title_full | The Ubiquitination System within Bacterial Host–Pathogen Interactions |
title_fullStr | The Ubiquitination System within Bacterial Host–Pathogen Interactions |
title_full_unstemmed | The Ubiquitination System within Bacterial Host–Pathogen Interactions |
title_short | The Ubiquitination System within Bacterial Host–Pathogen Interactions |
title_sort | ubiquitination system within bacterial host pathogen interactions |
topic | ubiquitination deubiquitinating enzymes (DUBs) effector protein host–pathogen interaction |
url | https://www.mdpi.com/2076-2607/9/3/638 |
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