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

Author

Listed:
  • Shuzhi Cui

    (University of Chinese Academy of Sciences, Chinese Academy of Sciences)

  • Tian Xia

    (University of Chinese Academy of Sciences, Chinese Academy of Sciences
    Institut Pasteur, Université Paris Cité)

  • 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
    Institut Pasteur, Université Paris Cité)

  • 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
    CIRI, Centre International de Recherche en Infectiologie, Univ Lyon, INSERM U1111, CNRS UMR5308, Université Claude Bernard Lyon 1, Ecole Normale Supérieure de Lyon)

  • 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
    Institut Pasteur, Université Paris Cité)

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.

Suggested Citation

  • 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 & Life, 2023. "NDP52 mediates an antiviral response to hepatitis B virus infection through Rab9-dependent lysosomal degradation pathway," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-44201-2
    DOI: 10.1038/s41467-023-44201-2
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    References listed on IDEAS

    as
    1. Byeong-Won Kim & Seung Beom Hong & Jun Hoe Kim & Do Hoon Kwon & Hyun Kyu Song, 2013. "Structural basis for recognition of autophagic receptor NDP52 by the sugar receptor galectin-8," Nature Communications, Nature, vol. 4(1), pages 1-8, June.
    2. Jacqueline Staring & Eleonore von Castelmur & Vincent A. Blomen & Lisa G. van den Hengel & Markus Brockmann & Jim Baggen & Hendrik Jan Thibaut & Joppe Nieuwenhuis & Hans Janssen & Frank J. M. van Kupp, 2017. "PLA2G16 represents a switch between entry and clearance of Picornaviridae," Nature, Nature, vol. 541(7637), pages 412-416, January.
    3. Yuya Nishida & Satoko Arakawa & Kenji Fujitani & Hirofumi Yamaguchi & Takeshi Mizuta & Toku Kanaseki & Masaaki Komatsu & Kinya Otsu & Yoshihide Tsujimoto & Shigeomi Shimizu, 2009. "Discovery of Atg5/Atg7-independent alternative macroautophagy," Nature, Nature, vol. 461(7264), pages 654-658, October.
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