ArticlePLoS pathogens2025
Netrin-1 inhibits the attachment and internalization of Hepatitis B virus for hepatocyte infection.
Article in PLoS pathogens, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
- Natural Alkaloids Against Liver Injury: Mechanistic Insights and Multi-Target Therapeutic Potential.Biomolecules · 2026Review
Corrections and comments
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Authors and funding
19 authors.
Funding
Abstract
Netrin-1, a secreted laminin-related protein, is increasingly recognized for its role in viral pathogenesis, alongside its established functions in neural guidance and immune regulation. We previously identified endothelial lipase (LIPG) as a host factor that facilitates hepatitis B virus (HBV) attachment via heparan sulfate proteoglycans (HSPGs) and/or the sodium taurocholate cotransporting polypeptide (NTCP). Through LIPG-based screening, we identified Netrin-1 as an LIPG-interacting protein, and synthetic peptides derived from Netrin-1 sequences exhibited potent anti-HBV activity. In primary human hepatocytes, Netrin-1 demonstrated antiviral activity against HBV, and in HepG2-NTCP-YFP cells, it inhibited viral attachment and internalization. Mechanistically, Netrin-1 binds to LIPG through heparin-binding motifs in its V and C domains, disrupting LIPG-HBV interactions and displacing LIPG from HSPGs. Furthermore, Netrin-1 binds to the extracellular domain of epidermal growth factor receptor (EGFR), abrogating NTCP-EGFR complex formation and inhibiting EGFR dimerization and phosphorylation, independently of HSPGs. In vivo, recombinant Netrin-1 suppressed the viral infection in humanized hepatocyte chimeric mice. These findings establish Netrin-1 as a multifunctional host factor that interferes with HBV entry, supporting the development of Netrin-1-based therapeutic strategies.
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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 Socratic graph.