ArticleNature communications2023
NDP52 mediates an antiviral response to hepatitis B virus infection through Rab9-dependent lysosomal degradation pathway.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Rab9 depletion enhances human adenovirus type 26 transduction efficiency through increased internalization and reduced late endosomal/lysosomal retention.PLoS pathogens · 2026Article
- Autophagy machinery as exploited by viruses.Autophagy reports · 2025Article
- CDC42 supports HBV entry by NTCP translocation to the plasma membrane and macropinocytosis.EMBO reports · 2025Article
- NDP52 and its emerging role in pathogenesis.Cell death & disease · 2025Review
- Hepatitis B and D virus entry.Nature reviews. Microbiology · 2025Review
- The HBV large envelope protein initiates virion assembly by recruiting capsids at membrane rich domains related to late endosome.Cellular and molecular life sciences : CMLS · 2025Article
- Class B scavenger receptor resists WSSV replication by recognizing the viral lipid molecule and promoting phagocytosis.Journal of virology · 2025Article
- Virus infection and vesicle trafficking.Frontiers in immunology · 2025Review
- CALCOCO2/NDP52 associates with RAB9 to initiate an antiviral response to hepatitis B virus infection through a lysosomal degradation pathway.Autophagy · 2024Article
- The role of galectins in the regulation of autophagy and inflammasome in host immunity.Seminars in immunopathology · 2024Review
Corrections and comments
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Authors and funding
20 authors at 5 institutions in 2 countries.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.