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Structures and distributions of SARS-CoV-2 spike proteins on intact virions

Author

Listed:
  • Zunlong Ke

    (Medical Research Council Laboratory of Molecular Biology)

  • Joaquin Oton

    (Medical Research Council Laboratory of Molecular Biology)

  • Kun Qu

    (Medical Research Council Laboratory of Molecular Biology)

  • Mirko Cortese

    (Molecular Virology, Heidelberg University)

  • Vojtech Zila

    (Virology, Heidelberg University)

  • Lesley McKeane

    (Medical Research Council Laboratory of Molecular Biology)

  • Takanori Nakane

    (Medical Research Council Laboratory of Molecular Biology)

  • Jasenko Zivanov

    (Medical Research Council Laboratory of Molecular Biology)

  • Christopher J. Neufeldt

    (Molecular Virology, Heidelberg University)

  • Berati Cerikan

    (Molecular Virology, Heidelberg University)

  • John M. Lu

    (Medical Research Council Laboratory of Molecular Biology)

  • Julia Peukes

    (Medical Research Council Laboratory of Molecular Biology)

  • Xiaoli Xiong

    (Medical Research Council Laboratory of Molecular Biology)

  • Hans-Georg Kräusslich

    (Virology, Heidelberg University
    Heidelberg Partner Site)

  • Sjors H. W. Scheres

    (Medical Research Council Laboratory of Molecular Biology)

  • Ralf Bartenschlager

    (Molecular Virology, Heidelberg University
    Heidelberg Partner Site
    German Cancer Research Center (DKFZ))

  • John A. G. Briggs

    (Medical Research Council Laboratory of Molecular Biology)

Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions are surrounded by a lipid bilayer from which spike (S) protein trimers protrude1. Heavily glycosylated S trimers bind to the angiotensin-converting enzyme 2 receptor and mediate entry of virions into target cells2–6. S exhibits extensive conformational flexibility: it modulates exposure of its receptor-binding site and subsequently undergoes complete structural rearrangement to drive fusion of viral and cellular membranes2,7,8. The structures and conformations of soluble, overexpressed, purified S proteins have been studied in detail using cryo-electron microscopy2,7,9–12, but the structure and distribution of S on the virion surface remain unknown. Here we applied cryo-electron microscopy and tomography to image intact SARS-CoV-2 virions and determine the high-resolution structure, conformational flexibility and distribution of S trimers in situ on the virion surface. These results reveal the conformations of S on the virion, and provide a basis from which to understand interactions between S and neutralizing antibodies during infection or vaccination.

Suggested Citation

  • Zunlong Ke & Joaquin Oton & Kun Qu & Mirko Cortese & Vojtech Zila & Lesley McKeane & Takanori Nakane & Jasenko Zivanov & Christopher J. Neufeldt & Berati Cerikan & John M. Lu & Julia Peukes & Xiaoli X, 2020. "Structures and distributions of SARS-CoV-2 spike proteins on intact virions," Nature, Nature, vol. 588(7838), pages 498-502, December.
    • Handle: RePEc:nat:nature:v:588:y:2020:i:7838:d:10.1038_s41586-020-2665-2
    DOI: 10.1038/s41586-020-2665-2
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