ArticleNature communications2024
Structural basis for hepatitis B virus restriction by a viral receptor homologue.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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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
13 citing papers in PubMed.
- Structural insight into sodium-dependent bile acid transport by members of the SLC10 family.Structure (London, England : 1993) · 2026Article
- Review
- Optimized bacterial expression of a synthetic BRIL antibody.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Membrane Fusion-Inspired Nanomaterials: Emerging Strategies for Infectious Disease and Cancer Diagnostics.Advanced healthcare materials · 2026Review
- Multistep receptor binding of the hepatitis B virus preS1 domain.Nature communications · 2026Article
- Structural mapping of NTCP distinguishes its dual functionality as a hepatitis B virus receptor and bile acid transporter.PLoS pathogens · 2026Article
- Onnamides A and B Suppress Hepatitis B Virus Transcription by Inhibiting Viral Promoter Activity.Marine drugs · 2026Article
- Amino acid substitutions at rheostat positions in the NaProtein science : a publication of the Protein Society · 2025Article
- Interaction between W41 of the hepatitis B virus preS1 surface peptide and Y146/F274 of the cellular receptor molecule NaMolecular pharmacology · 2025Article
- Screening of different species reveals cat hepatocytes support HBV infection.PLoS pathogens · 2025Article
- Hepatitis B and D virus entry.Nature reviews. Microbiology · 2025Review
- Engineering liver disease models in vitro: emerging trends and innovations.eGastroenterology · 2025Review
- Current status and challenges of therapeutic targets, novel drugs and delivery systems for hepatitis B: how far to our goal?Frontiers in cellular and infection microbiology · 2025Review
Corrections and comments
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Authors and funding
18 authors.
Funding
Abstract
Macaque restricts hepatitis B virus (HBV) infection because its receptor homologue, NTCP (mNTCP), cannot bind preS1 on viral surface. To reveal how mNTCP loses the viral receptor function, we here solve the cryo-electron microscopy structure of mNTCP. Superposing on the human NTCP (hNTCP)-preS1 complex structure shows that Arg158 of mNTCP causes steric clash to prevent preS1 from embedding onto the bile acid tunnel of NTCP. Cell-based mutation analysis confirms that only Gly158 permitted preS1 binding, in contrast to robust bile acid transport among mutations. As the second determinant, Asn86 on the extracellular surface of mNTCP shows less capacity to restrain preS1 from dynamic fluctuation than Lys86 of hNTCP, resulting in unstable preS1 binding. Additionally, presence of long-chain conjugated-bile acids in the tunnel induces steric hindrance with preS1 through their tailed-chain. This study presents structural basis in which multiple sites in mNTCP constitute a molecular barrier to strictly restrict HBV.
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