Abstract
The SARS-CoV-2 spike (S) protein, a primary target for COVID-19 vaccine development, presents its Receptor Binding Domain in two conformations, receptor-accessible “up” or receptor-inaccessible “down” states. Here we report that the commonly used stabilized S ectodomain construct “2P” is sensitive to cold temperature, and this cold sensitivity is abrogated in a “down” state–stabilized ectodomain. Our findings will impact structural, functional and vaccine studies that use SARS-CoV-2 S ectodomain.
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