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Published on: May 18, 2017
Legionella pneumophila-mediated host posttranslational modifications
Yi Yang1, Ligang Mei1, Jing Chen1
1School of Life Sciences, Chongqing University, Chongqing 401331, China.
Abstract:
Legionella pneumophila is a Gram-negative bacterium ubiquitously present in freshwater environments and causes a serious type of pneumonia called Legionnaires' disease. During infections, L. pneumophila releases over 300 effector proteins into host cells through an Icm/Dot type IV secretion system to manipulate the host defense system for survival within the host. Notably, certain effector proteins mediate posttranslational modifications (PTMs), serving as useful approaches exploited by L. pneumophila to modify host proteins. Some effectors catalyze the addition of host protein PTMs, while others mediate the removal of PTMs from host proteins. In this review, we summarize L. pneumophila effector-mediated PTMs of host proteins, including phosphorylation, ubiquitination, glycosylation, AMPylation, phosphocholination, methylation, and ADP-ribosylation, as well as dephosphorylation, deubiquitination, deAMPylation, deADP-ribosylation, dephosphocholination, and delipidation. We describe their molecular mechanisms and biological functions in the regulation of bacterial growth and Legionella-containing vacuole biosynthesis and in the disruption of host immune and defense machinery.
Insights
Legionella pneumophila manipulates host cells using effector proteins that add or remove posttranslational modifications (PTMs). This review details how these PTMs impact bacterial survival and host immune evasion.
Area of Science:
- Microbiology
- Cell Biology
- Biochemistry
Background:
- Legionella pneumophila, a Gram-negative bacterium, causes Legionnaires' disease pneumonia.
- It utilizes an Icm/Dot type IV secretion system to deliver over 300 effector proteins into host cells.
- These effectors manipulate host defenses for bacterial survival and replication.
Approach:
- This review summarizes effector-mediated posttranslational modifications (PTMs) of host proteins by L. pneumophila.
- It covers both the addition and removal of various PTMs, including phosphorylation, ubiquitination, glycosylation, AMPylation, phosphocholination, methylation, and ADP-ribosylation.
- The molecular mechanisms and biological functions of these PTMs are described.
Key Points:
- L. pneumophila effectors mediate diverse PTMs on host proteins, including phosphorylation, ubiquitination, glycosylation, AMPylation, phosphocholination, methylation, and ADP-ribosylation.
- Effectors also remove PTMs through dephosphorylation, deubiquitination, deAMPylation, deADP-ribosylation, dephosphocholination, and delipidation.
- These modifications are crucial for regulating bacterial growth, Legionella-containing vacuole biogenesis, and host immune disruption.
Conclusions:
- L. pneumophila extensively employs effector-mediated PTMs to subvert host cell processes.
- Understanding these PTMs provides insights into bacterial pathogenesis and host-pathogen interactions.
- Targeting these effector functions could offer novel therapeutic strategies against Legionnaires' disease.
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