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Structural conservation of HBV-like capsid proteins over hundreds of millions of years despite the shift from non-enveloped to enveloped life-style

Author

Listed:
  • Sara Pfister

    (Physical Chemistry, ETH Zurich)

  • Julius Rabl

    (Cryo-EM Knowledge hub, ETH Zurich)

  • Thomas Wiegand

    (Physical Chemistry, ETH Zurich
    Max-Planck-Institute for Chemical Energy Conversion
    RWTH Aachen University)

  • Simone Mattei

    (EMBL Imaging Centre, European Molecular Biology Laboratory, EMBL Heidelberg)

  • Alexander A. Malär

    (Physical Chemistry, ETH Zurich)

  • Lauriane Lecoq

    (UMR 5086 CNRS, Université de Lyon)

  • Stefan Seitz

    (German Cancer Research Center (DKFZ)
    University of Heidelberg)

  • Ralf Bartenschlager

    (German Cancer Research Center (DKFZ)
    University of Heidelberg)

  • Anja Böckmann

    (UMR 5086 CNRS, Université de Lyon)

  • Michael Nassal

    (University of Freiburg)

  • Daniel Boehringer

    (Cryo-EM Knowledge hub, ETH Zurich)

  • Beat H. Meier

    (Physical Chemistry, ETH Zurich)

Abstract

The discovery of nackednaviruses provided new insight into the evolutionary history of the hepatitis B virus (HBV): The common ancestor of HBV and nackednaviruses was non-enveloped and while HBV acquired an envelope during evolution, nackednaviruses remained non-enveloped. We report the capsid structure of the African cichlid nackednavirus (ACNDV), determined by cryo-EM at 3.7 Å resolution. This enables direct comparison with the known capsid structures of HBV and duck HBV, prototypic representatives of the mammalian and avian lineages of the enveloped Hepadnaviridae, respectively. The sequence identity with HBV is 24% and both the ACNDV capsid protein fold and the capsid architecture are very similar to those of the Hepadnaviridae and HBV in particular. Acquisition of the hepadnaviral envelope was thus not accompanied by a major change in capsid structure. Dynamic residues at the spike tip are tentatively assigned by solid-state NMR, while the C-terminal domain is invisible due to dynamics. Solid-state NMR characterization of the capsid structure reveals few conformational differences between the quasi-equivalent subunits of the ACNDV capsid and an overall higher capsid structural disorder compared to HBV. Despite these differences, the capsids of ACNDV and HBV are structurally highly similar despite the 400 million years since their separation.

Suggested Citation

  • Sara Pfister & Julius Rabl & Thomas Wiegand & Simone Mattei & Alexander A. Malär & Lauriane Lecoq & Stefan Seitz & Ralf Bartenschlager & Anja Böckmann & Michael Nassal & Daniel Boehringer & Beat H. Me, 2023. "Structural conservation of HBV-like capsid proteins over hundreds of millions of years despite the shift from non-enveloped to enveloped life-style," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
  • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-37068-w
    DOI: 10.1038/s41467-023-37068-w
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    References listed on IDEAS

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    1. Zongdi Feng & Lucinda Hensley & Kevin L. McKnight & Fengyu Hu & Victoria Madden & LiFang Ping & Sook-Hyang Jeong & Christopher Walker & Robert E. Lanford & Stanley M. Lemon, 2013. "A pathogenic picornavirus acquires an envelope by hijacking cellular membranes," Nature, Nature, vol. 496(7445), pages 367-371, April.
    2. Diego F. Gauto & Leandro F. Estrozi & Charles D. Schwieters & Gregory Effantin & Pavel Macek & Remy Sounier & Astrid C. Sivertsen & Elena Schmidt & Rime Kerfah & Guillaume Mas & Jacques-Philippe Colle, 2019. "Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex," Nature Communications, Nature, vol. 10(1), pages 1-12, December.
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