NDP52 mediates an antiviral response to hepatitis B virus infection through Rab9-dependent lysosomal degradation pathway

Shuzhi Cui, Tian Xia, Jianjin Zhao, Xiaoyu Ren, Tingtao Wu, Mireille Kameni, Xiaoju Guo, Li He, Jingao Guo, Aléria Duperray-Susini, Florence Levillayer, Jean-Marc Collard, Jin Zhong, Lifeng Pan, Frédéric Tangy, Pierre-Olivier Vidalain, Dongming Zhou, Yaming Jiu, Mathias Faure and Yu Wei ()
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Shuzhi Cui: University of Chinese Academy of Sciences, Chinese Academy of Sciences
Tian Xia: University of Chinese Academy of Sciences, Chinese Academy of Sciences
Jianjin Zhao: University of Chinese Academy of Sciences, Chinese Academy of Sciences
Xiaoyu Ren: University of Chinese Academy of Sciences, Chinese Academy of Sciences
Tingtao Wu: University of Chinese Academy of Sciences, Chinese Academy of Sciences
Mireille Kameni: University of Chinese Academy of Sciences, Chinese Academy of Sciences
Xiaoju Guo: University of Chinese Academy of Sciences, Chinese Academy of Sciences
Li He: University of Chinese Academy of Sciences, Chinese Academy of Sciences
Jingao Guo: University of Chinese Academy of Sciences, Chinese Academy of Sciences
Aléria Duperray-Susini: Institut Pasteur, Université Paris Cité
Florence Levillayer: Institut Pasteur, Université Paris Cité
Jean-Marc Collard: University of Chinese Academy of Sciences, Chinese Academy of Sciences
Jin Zhong: University of Chinese Academy of Sciences, Chinese Academy of Sciences
Lifeng Pan: Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences
Frédéric Tangy: Institut Pasteur, Université Paris Cité
Pierre-Olivier Vidalain: Institut Pasteur, Université Paris Cité
Dongming Zhou: Tianjin Medical University
Yaming Jiu: University of Chinese Academy of Sciences, Chinese Academy of Sciences
Mathias Faure: CIRI, Centre International de Recherche en Infectiologie, Univ Lyon, INSERM U1111, CNRS UMR5308, Université Claude Bernard Lyon 1, Ecole Normale Supérieure de Lyon
Yu Wei: University of Chinese Academy of Sciences, Chinese Academy of Sciences

Nature Communications, 2023, vol. 14, issue 1, 1-16

Abstract: Abstract Autophagy receptor NDP52 triggers bacterial autophagy against infection. However, the ability of NDP52 to protect against viral infection has not been established. We show that NDP52 binds to envelope proteins of hepatitis B virus (HBV) and triggers a degradation process that promotes HBV clearance. Inactivating NDP52 in hepatocytes results in decreased targeting of viral envelopes in the lysosome and increased levels of viral replication. NDP52 inhibits HBV at both viral entry and late replication stages. In contrast to NDP52-mediated bacterial autophagy, lysosomal degradation of HBV envelopes is independent of galectin 8 and ATG5. NDP52 forms complex with Rab9 and viral envelope proteins and links HBV to Rab9-dependent lysosomal degradation pathway. These findings reveal that NDP52 acts as a sensor for HBV infection, which mediates a unique antiviral response to eliminate the virus. This work also suggests direct roles for autophagy receptors in other lysosomal degradation pathways than canonical autophagy.

Date: 2023
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DOI: 10.1038/s41467-023-44201-2

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