Phosphorylation of caspases by a bacterial kinase inhibits host programmed cell death

Jinli Ge, Ying Wang, Xueyu Li, Qian Lu, Hangqian Yu, Hongtao Liu, Kelong Ma, Xuming Deng, Zhao-Qing Luo, Xiaoyun Liu () and Jiazhang Qiu ()
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Jinli Ge: Jilin University
Ying Wang: Peking University Health Science Center
Xueyu Li: Jilin University
Qian Lu: Jilin University
Hangqian Yu: Jilin University
Hongtao Liu: Jilin University
Kelong Ma: Jilin University
Xuming Deng: Jilin University
Zhao-Qing Luo: Purdue University
Xiaoyun Liu: Peking University Health Science Center
Jiazhang Qiu: Jilin University

Nature Communications, 2024, vol. 15, issue 1, 1-14

Abstract: Abstract The intracellular bacterial pathogen Legionella pneumophila utilizes the Dot/Icm system to translocate over 330 effectors into the host cytosol. These virulence factors modify a variety of cell processes, including pathways involved in cell death and survival, to promote bacterial proliferation. Here, we show that the effector LegK3 is a eukaryotic-like Ser/Thr kinase that functions to suppress host apoptosis. Mechanistically, LegK3 directly phosphorylates multiple caspases involved in apoptosis signaling, including Caspase-3, Caspase-7, and Caspase-9. LegK3-induced phosphorylation of these caspases occurs at serine (Ser29 in Caspase-3 and Ser199 in Caspase-7) or threonine (Thr102 in Caspase-9) residues located in the prodomain or interdomain linkers. These modifications interfere with the suitability of the caspases as the substrates of initiator caspases or upstream regulators without impacting their proteolytic activity. Collectively, our study reveals a novel strategy used by L. pneumophila to maintain the integrity of infected cells for its intracellular growth.

Date: 2024
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DOI: 10.1038/s41467-024-52817-1

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