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• W3119250802 abstract "Abstract The trimeric spike (S) protein of SARS-CoV-2 is the primary focus of most vaccine design and development efforts. Due to intrinsic instability typical of class I fusion proteins, S tends to prematurely refold to the post-fusion conformation, compromising immunogenic properties and prefusion trimer yields. To support ongoing vaccine development efforts, we report the structure-based design of soluble S trimers with increased yields and stabilities, based on introduction of single point mutations and disulfide-bridges. We identify regions critical for stability: the heptad repeat region 1, the SD1 domain and position 614 in SD2. We combine a minimal selection of mostly interprotomeric mutations to create a stable S-closed variant with a 6.4-fold higher expression than the parental construct while no longer containing a heterologous trimerization domain. The cryo-EM structure reveals a correctly folded, predominantly closed pre-fusion conformation. Highly stable and well producing S protein and the increased understanding of S protein structure will support vaccine development and serological diagnostics." @default.
• W3119250802 created "2021-01-18" @default.
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• W3119250802 date "2021-01-11" @default.
• W3119250802 modified "2023-10-05" @default.
• W3119250802 title "Stabilizing the closed SARS-CoV-2 spike trimer" @default.
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• W3119250802 doi "https://doi.org/10.1038/s41467-020-20321-x" @default.
• W3119250802 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7801441" @default.
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• W3119250802 hasPublicationYear "2021" @default.
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