Structural analysis of full-length SARS-CoV-2 spike protein from an advanced vaccine candidate

  1. Sandhya Bangaru
  2. Gabriel Ozorowski
  3. Hannah L. Turner
  4. Aleksandar Antanasijevic
  5. Deli Huang
  6. Xiaoning Wang
  7. Jonathan L. Torres
  8. Jolene K. Diedrich
  9. Jing-Hui Tian
  10. Alyse D. Portnoff
  11. Nita Patel
  12. Michael J. Massare
  13. John R. Yates
  14. David Nemazee
  15. James C. Paulson
  16. Greg Glenn
  17. Gale Smith
  18. Andrew B. Ward

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Abstract

Much effort is being targeted at developing vaccines that will provide protection against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). A trimeric spike protein that decorates the virus is a primary target of the host immune system and the focus of vaccine development. Bangaru et al. present the structure of a leading vaccine candidate: a full-length spike protein with some modifications aimed at enhancing stability that is formulated in polysorbate 80 detergent. The study confirms that the full-length immunogen is in a stable prefusion conformation and provides a basis for understanding immune responses to the vaccine.

Science , this issue p. 1089

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  1. Version published to 10.1126/science.abe1502
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    SciScore for 10.1101/2020.08.06.234674: (What is this?)

    Please note, not all rigor criteria are appropriate for all manuscripts.

    Table 1: Rigor

    Institutional Review Board Statementnot detected.
    Randomizationnot detected.
    Blindingnot detected.
    Power Analysisnot detected.
    Sex as a biological variablenot detected.

    Table 2: Resources

    Software and Algorithms
    SentencesResources
    Materials and Methods:
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    suggested: None

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    Results from JetFighter: Please consider improving the rainbow (“jet”) colormap(s) used on page 37. At least one figure is not accessible to readers with colorblindness and/or is not true to the data, i.e. not perceptually uniform.

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  3. Version published to 10.1101/2020.08.06.234674v1 on bioRxiv