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SARS-CoV-2 spike conformation determines plasma neutralizing activity.

John E Bowen1, Alexandra C Walls1,2, Anshu Joshi1

  • 1Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.

Biorxiv : the Preprint Server for Biology
|January 4, 2022
PubMed
Summary

Vaccines encoding prefusion-stabilized spike proteins generate stronger antibody responses against SARS-CoV-2. This prefusion spike conformation enhances protection and guides future vaccine design for improved durability and variant resilience.

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Area of Science:

  • Immunology
  • Vaccinology
  • Structural Biology

Background:

  • The SARS-CoV-2 spike (S) glycoprotein's conformation is critical for viral entry and a key target for vaccines and antibodies.
  • Understanding how different vaccine strategies and natural infection impact S glycoprotein conformation-specific antibody responses is crucial for improving vaccine efficacy.

Approach:

  • Compared plasma antibody responses elicited by six global COVID-19 vaccines and natural infection.
  • Analyzed binding titers and neutralizing activity against prefusion-stabilized S glycoprotein and its subunits.

Key Points:

  • Vaccines encoding prefusion-stabilized S glycoprotein induced significantly higher binding antibody titers compared to other vaccines or infection.
  • Prefusion S binding titers strongly correlated with plasma neutralizing activity, indicating enhanced protection.
  • Neutralizing activity is primarily directed against the prefusion S, particularly the S1 subunit.
  • Antibodies targeting the receptor-binding domain (RBD) mediate cross-neutralization of SARS-CoV-2 variants.

Conclusions:

  • Physical stabilization of the prefusion S conformation enhances protective antibody responses against SARS-CoV-2.
  • Future S glycoprotein engineering efforts should focus on prefusion stabilization to develop more durable vaccines with increased resilience to emerging variants.