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TitleStructural and biochemical rationale for Beta variant protein booster vaccine broad cross-neutralization of SARS-CoV-2.
Journal, issue, pagesSci Rep, Vol. 14, Issue 1, Page 2038, Year 2024
Publish dateJan 23, 2024
AuthorsEduardo M Bruch / Shaolong Zhu / Lisa Szymkowicz / Taylor Blake / Tara Kiss / D Andrew James / Alexey Rak / Kartik Narayan / Matthew T Balmer / Roman M Chicz /
PubMed AbstractSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2), responsible for the COVID-19 pandemic, uses a surface expressed trimeric spike glycoprotein for cell entry. This trimer is the primary ...Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), responsible for the COVID-19 pandemic, uses a surface expressed trimeric spike glycoprotein for cell entry. This trimer is the primary target for neutralizing antibodies making it a key candidate for vaccine development. During the global pandemic circulating variants of concern (VOC) caused several waves of infection, severe disease, and death. The reduced efficacy of the ancestral trimer-based vaccines against emerging VOC led to the need for booster vaccines. Here we present a detailed characterization of the Sanofi Beta trimer, utilizing cryo-EM for structural elucidation. We investigate the conformational dynamics and stabilizing features using orthogonal SPR, SEC, nanoDSF, and HDX-MS techniques to better understand how this antigen elicits superior broad neutralizing antibodies as a variant booster vaccine. This structural analysis confirms the Beta trimer preference for canonical quaternary structure with two RBD in the up position and the reversible equilibrium between the canonical spike and open trimer conformations. Moreover, this report provides a better understanding of structural differences between spike antigens contributing to differential vaccine efficacy.
External linksSci Rep / PubMed:38263191 / PubMed Central
MethodsEM (single particle)
Resolution2.75 - 2.85 Å
Structure data

41725

8tyl

EMDB-41725, PDB-8tyl:
Structural and biochemical rationale for Beta variant protein booster vaccine broad cross-neutralization of SARS-CoV-2
Method: EM (single particle) / Resolution: 2.85 Å

41727

8tyo

EMDB-41727, PDB-8tyo:
Structural and biochemical rationale for Beta variant protein booster vaccine broad cross-neutralization of SARS-CoV-2
Method: EM (single particle) / Resolution: 2.75 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • severe acute respiratory syndrome coronavirus 2
KeywordsVIRAL PROTEIN / Spike / trimer / surface

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