Burkholderia pseudomallei BipD modulates host mitophagy to evade killing

Dongqi Nan, Chenglong Rao, Zhiheng Tang, Wenbo Yang, Pan Wu, Jiangao Chen, Yupei Xia, Jingmin Yan, Wenzheng Liu, Ziyuan Zhang, Zhiqiang Hu, Hai Chen, Yaling Liao, Xuhu Mao (), Xiaoyun Liu (), Quanming Zou () and Qian Li ()
Additional contact information
Dongqi Nan: Army Medical University (Third Military Medical University)
Chenglong Rao: Army Medical University (Third Military Medical University)
Zhiheng Tang: Peking University Health Science Center
Wenbo Yang: Army Medical University (Third Military Medical University)
Pan Wu: Army Medical University (Third Military Medical University)
Jiangao Chen: Army Medical University (Third Military Medical University)
Yupei Xia: Army Medical University (Third Military Medical University)
Jingmin Yan: Army Medical University (Third Military Medical University)
Wenzheng Liu: Army Medical University (Third Military Medical University)
Ziyuan Zhang: Army Medical University (Third Military Medical University)
Zhiqiang Hu: Army Medical University (Third Military Medical University)
Hai Chen: Sanya People’s Hospital
Yaling Liao: Army Medical University (Third Military Medical University)
Xuhu Mao: Army Medical University (Third Military Medical University)
Xiaoyun Liu: Peking University Health Science Center
Quanming Zou: Army Medical University (Third Military Medical University)
Qian Li: Army Medical University (Third Military Medical University)

Nature Communications, 2024, vol. 15, issue 1, 1-17

Abstract: Abstract Mitophagy is critical for mitochondrial quality control and function to clear damaged mitochondria. Here, we found that Burkholderia pseudomallei maneuvered host mitophagy for its intracellular survival through the type III secretion system needle tip protein BipD. We identified BipD, interacting with BTB-containing proteins KLHL9 and KLHL13 by binding to the Back and Kelch domains, recruited NEDD8 family RING E3 ligase CUL3 in response to B. pseudomallei infection. Although evidently not involved in regulation of infectious diseases, KLHL9/KLHL13/CUL3 E3 ligase complex was essential for BipD-dependent ubiquitination of mitochondria in mouse macrophages. Mechanistically, we discovered the inner mitochondrial membrane IMMT via host ubiquitome profiling as a substrate of KLHL9/KLHL13/CUL3 complex. Notably, K63-linked ubiquitination of IMMT K211 was required for initiating host mitophagy, thereby reducing mitochondrial ROS production. Here, we show a unique mechanism used by bacterial pathogens that hijacks host mitophagy for their survival.

Date: 2024
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DOI: 10.1038/s41467-024-48824-x

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