ArticleStructure (London, England : 1993)2026
Cryo-EM structures of HBV capsids from human cells at near-atomic resolution.
Article in Structure (London, England : 1993), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Atomic resolution structure of human papillomavirus bound to heparin.Nature communications · 2026Article
- Assembly-active and -inactive forms of HBV capsid protein provide distinctly different binding sites for capsid assembly modulators.bioRxiv : the preprint server for biology · 2026Article
- Protocol for purifying recombinant HBV capsids from HepG2 cells and comparative phosphorylation analysis by phosphate-affinity SDS-PAGE.STAR protocols · 2026Article
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Authors and funding
11 authors.
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Abstract
HBV causes chronic infections that can lead to severe liver disease, yet current treatments rarely achieve a cure. The HBV capsid is a critical therapeutic target, but structural insights have largely relied on E. coli-derived particles lacking native modifications. Here, we present near-atomic resolution cryo-electron microscopy (EM) structures of HBV capsids purified from human embryonic kidney (HEK-293T) cells, capturing authentic architecture and post-translational modifications. A hydrophobic pocket at the intradimer interface harbors lipid-like densities corresponding to stearic and palmitic acids, confirmed by gas chromatography-mass spectrometry. Molecular dynamics simulations revealed that pocket accessibility is regulated by rotamer states of Lys96, Phe97, and Gln99, supporting an induced fit model of fatty acid binding. Reduced phosphorylation and increased RNA content further modulate capsid conformation and pocket openness. These findings highlight the dynamic regulation of HBV capsid structure and provide a framework for understanding how capsid conformational dynamics contribute to viral assembly and envelopment.
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