Legionella maintains host cell ubiquitin homeostasis by effectors with unique catalytic mechanisms

Jiaqi Fu, Siying Li, Hongxin Guan, Chuang Li, Yan-Bo Zhao, Tao-Tao Chen, Wei Xian, Zhengrui Zhang, Yao Liu, Qingtian Guan, Jingting Wang, Qiuhua Lu, Lina Kang, Si-Ru Zheng, Jinyu Li, Shoujing Cao, Chittaranjan Das, Xiaoyun Liu (), Lei Song (), Songying Ouyang () and Zhao-Qing Luo ()
Additional contact information
Jiaqi Fu: The First Hospital of Jilin University
Siying Li: The First Hospital of Jilin University
Hongxin Guan: Fujian Normal University
Chuang Li: Purdue University
Yan-Bo Zhao: Fujian Normal University
Tao-Tao Chen: Fujian Normal University
Wei Xian: Peking University Health Science Center
Zhengrui Zhang: Purdue University
Yao Liu: Purdue University
Qingtian Guan: The First Hospital of Jilin University
Jingting Wang: Fujian Normal University
Qiuhua Lu: Fujian Normal University
Lina Kang: Fujian Normal University
Si-Ru Zheng: Fujian Normal University
Jinyu Li: Fuzhou University
Shoujing Cao: Fuzhou University
Chittaranjan Das: Purdue University
Xiaoyun Liu: Peking University Health Science Center
Lei Song: The First Hospital of Jilin University
Songying Ouyang: Fujian Normal University
Zhao-Qing Luo: Purdue University

Nature Communications, 2024, vol. 15, issue 1, 1-13

Abstract: Abstract The intracellular bacterial pathogen Legionella pneumophila modulates host cell functions by secreting multiple effectors with diverse biochemical activities. In particular, effectors of the SidE family interfere with host protein ubiquitination in a process that involves production of phosphoribosyl ubiquitin (PR-Ub). Here, we show that effector LnaB converts PR-Ub into ADP-ribosylated ubiquitin, which is further processed to ADP-ribose and functional ubiquitin by the (ADP-ribosyl)hydrolase MavL, thus maintaining ubiquitin homeostasis in infected cells. Upon being activated by actin, LnaB also undergoes self-AMPylation on tyrosine residues. The activity of LnaB requires a motif consisting of Ser, His and Glu (SHxxxE) present in a large family of toxins from diverse bacterial pathogens. Thus, our study sheds light on the mechanisms by which a pathogen maintains ubiquitin homeostasis and identifies a family of enzymes capable of protein AMPylation.

Date: 2024
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DOI: 10.1038/s41467-024-50311-2

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