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

Here, the authors demonstrate that the Legionella pneumophila T4SS effector protein Lpg2370 is a Ser/Thr kinase and a toxin of a tripartite HipBST toxin-antitoxin (TA) system. Structural data and biochemical analysis provide detailed insights into the toxin neutralization mechanism in the HipBST TA.

Bibliographic Details
Main Authors: Xiangkai Zhen, Yongyu Wu, Jinli Ge, Jiaqi Fu, Le Ye, Niannian Lin, Zhijie Huang, Zihe Liu, Zhao-qing Luo, Jiazhang Qiu, Songying Ouyang
Format: Article
Language:English
Published: Nature Portfolio 2022-07-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-022-32049-x
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author Xiangkai Zhen
Yongyu Wu
Jinli Ge
Jiaqi Fu
Le Ye
Niannian Lin
Zhijie Huang
Zihe Liu
Zhao-qing Luo
Jiazhang Qiu
Songying Ouyang
author_facet Xiangkai Zhen
Yongyu Wu
Jinli Ge
Jiaqi Fu
Le Ye
Niannian Lin
Zhijie Huang
Zihe Liu
Zhao-qing Luo
Jiazhang Qiu
Songying Ouyang
author_sort Xiangkai Zhen
collection DOAJ
description Here, the authors demonstrate that the Legionella pneumophila T4SS effector protein Lpg2370 is a Ser/Thr kinase and a toxin of a tripartite HipBST toxin-antitoxin (TA) system. Structural data and biochemical analysis provide detailed insights into the toxin neutralization mechanism in the HipBST TA.
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spelling doaj.art-1487df0573c54c1a849daa2b17a704832022-12-22T02:05:49ZengNature PortfolioNature Communications2041-17232022-07-0113111410.1038/s41467-022-32049-xMolecular mechanism of toxin neutralization in the HipBST toxin-antitoxin system of Legionella pneumophilaXiangkai Zhen0Yongyu Wu1Jinli Ge2Jiaqi Fu3Le Ye4Niannian Lin5Zhijie Huang6Zihe Liu7Zhao-qing Luo8Jiazhang Qiu9Songying Ouyang10Provincial University Key Laboratory of Cellular Stress Response and Metabolic Regulation, the Key Laboratory of Innate Immune Biology of Fujian Province, Biomedical Research Center of South China, Key Laboratory of OptoElectronic Science and Technology for Medicine of the Ministry of Education, College of Life Sciences, Fujian Normal UniversityProvincial University Key Laboratory of Cellular Stress Response and Metabolic Regulation, the Key Laboratory of Innate Immune Biology of Fujian Province, Biomedical Research Center of South China, Key Laboratory of OptoElectronic Science and Technology for Medicine of the Ministry of Education, College of Life Sciences, Fujian Normal UniversityState Key Laboratory for Zoonotic Diseases, College of Veterinary Medicine, Jilin UniversityPurdue Institute for Inflammation, Immunology and Infectious Disease and Department of Biological Sciences, Purdue UniversityProvincial University Key Laboratory of Cellular Stress Response and Metabolic Regulation, the Key Laboratory of Innate Immune Biology of Fujian Province, Biomedical Research Center of South China, Key Laboratory of OptoElectronic Science and Technology for Medicine of the Ministry of Education, College of Life Sciences, Fujian Normal UniversityProvincial University Key Laboratory of Cellular Stress Response and Metabolic Regulation, the Key Laboratory of Innate Immune Biology of Fujian Province, Biomedical Research Center of South China, Key Laboratory of OptoElectronic Science and Technology for Medicine of the Ministry of Education, College of Life Sciences, Fujian Normal UniversityProvincial University Key Laboratory of Cellular Stress Response and Metabolic Regulation, the Key Laboratory of Innate Immune Biology of Fujian Province, Biomedical Research Center of South China, Key Laboratory of OptoElectronic Science and Technology for Medicine of the Ministry of Education, College of Life Sciences, Fujian Normal UniversityProvincial University Key Laboratory of Cellular Stress Response and Metabolic Regulation, the Key Laboratory of Innate Immune Biology of Fujian Province, Biomedical Research Center of South China, Key Laboratory of OptoElectronic Science and Technology for Medicine of the Ministry of Education, College of Life Sciences, Fujian Normal UniversityPurdue Institute for Inflammation, Immunology and Infectious Disease and Department of Biological Sciences, Purdue UniversityState Key Laboratory for Zoonotic Diseases, College of Veterinary Medicine, Jilin UniversityProvincial University Key Laboratory of Cellular Stress Response and Metabolic Regulation, the Key Laboratory of Innate Immune Biology of Fujian Province, Biomedical Research Center of South China, Key Laboratory of OptoElectronic Science and Technology for Medicine of the Ministry of Education, College of Life Sciences, Fujian Normal UniversityHere, the authors demonstrate that the Legionella pneumophila T4SS effector protein Lpg2370 is a Ser/Thr kinase and a toxin of a tripartite HipBST toxin-antitoxin (TA) system. Structural data and biochemical analysis provide detailed insights into the toxin neutralization mechanism in the HipBST TA.https://doi.org/10.1038/s41467-022-32049-x
spellingShingle Xiangkai Zhen
Yongyu Wu
Jinli Ge
Jiaqi Fu
Le Ye
Niannian Lin
Zhijie Huang
Zihe Liu
Zhao-qing Luo
Jiazhang Qiu
Songying Ouyang
Molecular mechanism of toxin neutralization in the HipBST toxin-antitoxin system of Legionella pneumophila
Nature Communications
title Molecular mechanism of toxin neutralization in the HipBST toxin-antitoxin system of Legionella pneumophila
title_full Molecular mechanism of toxin neutralization in the HipBST toxin-antitoxin system of Legionella pneumophila
title_fullStr Molecular mechanism of toxin neutralization in the HipBST toxin-antitoxin system of Legionella pneumophila
title_full_unstemmed Molecular mechanism of toxin neutralization in the HipBST toxin-antitoxin system of Legionella pneumophila
title_short Molecular mechanism of toxin neutralization in the HipBST toxin-antitoxin system of Legionella pneumophila
title_sort molecular mechanism of toxin neutralization in the hipbst toxin antitoxin system of legionella pneumophila
url https://doi.org/10.1038/s41467-022-32049-x
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