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Updated: Nov 21, 2025

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Stabilizing the closed SARS-CoV-2 spike trimer.

Jarek Juraszek1, Lucy Rutten1, Sven Blokland1

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|January 12, 2021
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Summary
This summary is machine-generated.

Researchers engineered a more stable SARS-CoV-2 spike (S) protein trimer for vaccine development. This improved S protein design enhances yield and stability, crucial for effective immunogens and diagnostics.

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Area of Science:

  • Virology
  • Structural Biology
  • Immunology

Background:

  • The SARS-CoV-2 spike (S) protein is a key target for vaccines.
  • Class I fusion proteins like S are inherently unstable, often refolding prematurely.
  • This instability reduces immunogenicity and complicates production of prefusion trimers.

Purpose of the Study:

  • To design stabilized, soluble SARS-CoV-2 S protein trimers.
  • To enhance S protein yields and immunogenic properties for vaccine development.
  • To elucidate the structural basis of S protein stability.

Main Methods:

  • Structure-based design incorporating single point mutations and disulfide bridges.
  • Identification of critical regions for S protein stability (HR1, SD1, position 614).
  • Cryo-electron microscopy (cryo-EM) to determine the structure of the designed S variant.

Main Results:

  • Developed a stable, closed S-closed variant with 6.4-fold higher expression than the parent construct.
  • Introduced interprotomeric mutations and disulfide bridges for enhanced stability.
  • Cryo-EM confirmed a correctly folded, predominantly closed prefusion conformation.

Conclusions:

  • Engineered soluble S protein trimers exhibit significantly improved stability and expression.
  • Understanding S protein structure-stability relationships aids vaccine design.
  • The stable S protein variant supports vaccine development and serological diagnostics.