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- W3197484911 abstract "The SARS-CoV-2 spike is the primary target of virus-neutralizing antibodies and critical to the development of effective vaccines against COVID-19. Here, we demonstrate that the prefusion-stabilized two-proline S2P spike-widely employed for laboratory work and clinical studies-unfolds when stored at 4 °C, physiological pH, as observed by electron microscopy (EM) and differential scanning calorimetry, but that its trimeric, native-like conformation can be reacquired by low pH treatment. When stored for approximately 1 week, this unfolding does not significantly alter antigenic characteristics; however, longer storage diminishes antibody binding, and month-old spike elicits virtually no neutralization in mice despite inducing high ELISA-binding titers. Cryo-EM structures reveal the folded fraction of spike to decrease with aging; however, its structure remains largely similar, although with varying mobility of the receptor-binding domain. Thus, the SARS-CoV-2 spike is susceptible to unfolding, which affects immunogenicity, highlighting the need to monitor its integrity." @default.
- W3197484911 created "2021-09-13" @default.
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- W3197484911 date "2021-10-01" @default.
- W3197484911 modified "2023-10-06" @default.
- W3197484911 title "SARS-CoV-2 S2P spike ages through distinct states with altered immunogenicity" @default.
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- W3197484911 doi "https://doi.org/10.1016/j.jbc.2021.101127" @default.
- W3197484911 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8393506" @default.
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