自噬
乙型肝炎病毒
病毒学
生物
病毒复制
溶酶体
病毒
酶
生物化学
细胞凋亡
作者
Shuzhi Cui,Tian Xia,Jianjin Zhao,Xiaoyu Ren,Tingtao Wu,Mireille Kameni,Xiaoju Guo,He Li,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,Yu Wei
标识
DOI:10.1038/s41467-023-44201-2
摘要
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.
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