ArticleScience advances2024
Structural basis for nuclear import of hepatitis B virus (HBV) nucleocapsid core.
Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- SPSignal: a web tool for structure-assisted prediction of nuclear localization and nuclear export signals in proteins.Nucleic acids research · 2026Article
- Insight into the Biology of Hepatitis B Virus and Recent Therapeutic Approaches.Current microbiology · 2026Review
- A multivalent adaptor mechanism drives the nuclear import of proteasomes.Nature communications · 2026Article
- Ran modulates allosteric crosstalk between importin β surfaces.Nature communications · 2025Article
- Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025Review
- The localisation and stability of the CENP-F protein are regulated by importin beta and microtubules in mitotic cells.Scientific reports · 2025Article
- Hepatitis B and D virus entry.Nature reviews. Microbiology · 2025Review
- Article
- HBc: the multifunctional architect of HBV replication, immune evasion, and therapeutic innovation.Frontiers in immunology · 2025Review
- Hepatitis B virus entry, assembly, and egress.Microbiology and molecular biology reviews : MMBR · 2024Review
- Channel width modulates the permeability of DNA origami-based nuclear pore mimics.Science advances · 2024Article
- Single Acetylation-mimetic Mutation in TDP-43 Nuclear Localization Signal Disrupts Importin α1/β Signaling.Journal of molecular biology · 2024Article
- A nucleosome switch primes Hepatitis B Virus infection.bioRxiv : the preprint server for biology · 2024Article
- Channel width modulates the permeability of DNA origami based nuclear pore mimics.bioRxiv : the preprint server for biology · 2024Article
Corrections and comments
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Authors and funding
14 authors at 4 institutions in 1 country.
Funding
Abstract
Nuclear import of the hepatitis B virus (HBV) nucleocapsid is essential for replication that occurs in the nucleus. The ~360-angstrom HBV capsid translocates to the nuclear pore complex (NPC) as an intact particle, hijacking human importins in a reaction stimulated by host kinases. This paper describes the mechanisms of HBV capsid recognition by importins. We found that importin α1 binds a nuclear localization signal (NLS) at the far end of the HBV coat protein Cp183 carboxyl-terminal domain (CTD). This NLS is exposed to the capsid surface through a pore at the icosahedral quasi-sixfold vertex. Phosphorylation at serine-155, serine-162, and serine-170 promotes CTD compaction but does not affect the affinity for importin α1. The binding of 30 importin α1/β1 augments HBV capsid diameter to ~620 angstroms, close to the maximum size trafficable through the NPC. We propose that phosphorylation favors CTD externalization and prompts its compaction at the capsid surface, exposing the NLS to importins.
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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.