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Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy

Author

Listed:
  • B. Böttcher

    (Medical Research Council Laboratory of Molecular Biology
    Universität Freiburg)

  • S. A. Wynne

    (Medical Research Council Laboratory of Molecular Biology)

  • R. A. Crowther

    (Medical Research Council Laboratory of Molecular Biology)

Abstract

Hepatitis B virus, a major human pathogen with an estimated 300 million carriers worldwide, can lead to cirrhosis and liver cancer in cases of chronic infection. The virus consists of an inner nucleocapsid or core, surrounded by a lipid envelope containing virally encoded surface proteins. The core protein, when expressed in bacteria, assembles into core shell particles, closely resembling the native core of the virus. Here we use electron cryomicroscopy to solve the structure of the core protein to 7.4 Å resolution. Images of about 6,400 individual particles from 34 micrographs at different levels of defocus were combined, imposing icosahedral symmetry. The three-dimensional map reveals the complete fold of the polypeptide chain, which is quite unlike previously solved viral capsid proteins and is largely α-helical. The dimer clustering of subunits produces spikes on the surface of the shell, which consist of radial bundles of four long α-helices. Our model implies that the sequence corresponding to the immunodominant region of the core protein lies at the tip of the spike and also explains other properties of the core protein.

Suggested Citation

  • B. Böttcher & S. A. Wynne & R. A. Crowther, 1997. "Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy," Nature, Nature, vol. 386(6620), pages 88-91, March.
  • Handle: RePEc:nat:nature:v:386:y:1997:i:6620:d:10.1038_386088a0
    DOI: 10.1038/386088a0
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    Cited by:

    1. Bhakta, Sayan & van Heel, Marin, 2024. "Single-Particle Cryo-EM: What happens inside the Black Box?," OSF Preprints 5empt, Center for Open Science.
    2. Lauriane Lecoq & Louis Brigandat & Rebecca Huber & Marie-Laure Fogeron & Shishan Wang & Marie Dujardin & Mathilde Briday & Thomas Wiegand & Morgane Callon & Alexander Malär & David Durantel & Dara Bur, 2023. "Molecular elucidation of drug-induced abnormal assemblies of the hepatitis B virus capsid protein by solid-state NMR," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    3. Jianfang Liu & Ewan K. S. McRae & Meng Zhang & Cody Geary & Ebbe Sloth Andersen & Gang Ren, 2024. "Non-averaged single-molecule tertiary structures reveal RNA self-folding through individual-particle cryo-electron tomography," Nature Communications, Nature, vol. 15(1), pages 1-18, December.

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