Molecular mechanism of toxin neutralization in the HipBST toxin-antitoxin system of Legionella pneumophila

Xiangkai Zhen, Yongyu Wu, Jinli Ge, Jiaqi Fu, Le Ye, Niannian Lin, Zhijie Huang, Zihe Liu, Zhao-qing Luo, Jiazhang Qiu () and Songying Ouyang ()
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Xiangkai Zhen: Fujian Normal University
Yongyu Wu: Fujian Normal University
Jinli Ge: Jilin University
Jiaqi Fu: Purdue University
Le Ye: Fujian Normal University
Niannian Lin: Fujian Normal University
Zhijie Huang: Fujian Normal University
Zihe Liu: Fujian Normal University
Zhao-qing Luo: Purdue University
Jiazhang Qiu: Jilin University
Songying Ouyang: Fujian Normal University

Nature Communications, 2022, vol. 13, issue 1, 1-14

Abstract: Abstract Toxin-antitoxin (TA) systems are ubiquitous genetic modules in bacteria and archaea. Here, we perform structural and biochemical characterization of the Legionella pneumophila effector Lpg2370, demonstrating that it is a Ser/Thr kinase. Together with two upstream genes, lpg2370 constitutes the tripartite HipBST TA. Notably, the toxin Lpg2370 (HipTLp) and the antitoxin Lpg2369 (HipSLp) correspond to the C-terminus and N-terminus of HipA from HipBA TA, respectively. By determining crystal structures of autophosphorylated HipTLp, its complex with AMP-PNP, and the structure of HipTLp-HipSLp complex, we identify residues in HipTLp critical for ATP binding and those contributing to its interactions with HipSLp. Structural analysis reveals that HipSLp binding induces a loop-to-helix shift in the P-loop of HipTLp, leading to the blockage of ATP binding and inhibition of the kinase activity. These findings establish the L. pneumophila effector Lpg2370 as the HipBST TA toxin and elucidate the molecular basis for HipT neutralization in HipBST TA.

Date: 2022
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DOI: 10.1038/s41467-022-32049-x

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