National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
120553
United States
Citation
Journal: bioRxiv / Year: 2020 Title: Closing coronavirus spike glycoproteins by structure-guided design. Authors: Matthew McCallum / Alexandra C Walls / Davide Corti / David Veesler / Abstract: The recent spillover of SARS-CoV-2 in the human population resulted in the ongoing COVID-19 pandemic which has already caused 4.9 million infections and more than 326,000 fatalities. To initiate ...The recent spillover of SARS-CoV-2 in the human population resulted in the ongoing COVID-19 pandemic which has already caused 4.9 million infections and more than 326,000 fatalities. To initiate infection the SARS-CoV-2 spike (S) glycoprotein promotes attachment to the host cell surface, determining host and tissue tropism, and fusion of the viral and host membranes. Although SARS-CoV-2 S is the main target of neutralizing antibodies and the focus of vaccine design, its stability and conformational dynamics are limiting factors for developing countermeasures against this virus. We report here the design of a prefusion SARS-CoV-2 S ectodomain trimer construct covalently stabilized in the closed conformation. Structural and antigenicity analysis showed we successfully shut S in the closed state without otherwise altering its architecture. Finally, we show that this engineering strategy is applicable to other β-coronavirus S glycoproteins and might become an important tool for vaccine design, structural biology, serology and immunology studies.
History
Deposition
May 29, 2020
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Header (metadata) release
Aug 19, 2020
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Map release
Aug 19, 2020
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Update
Jan 27, 2021
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Current status
Jan 27, 2021
Processing site: RCSB / Status: Released
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