Cold sensitivity of the SARS-CoV-2 spike ectodomain
R. J. Edwards, K. Mansouri, V. Stalls, K. Manne, B. Watts, R. Parks, K. Janowska, S. M. C. Gobeil, M. Kopp, D. Li, X. Lu, Z. Mu, M. Deyton, T. Oguin, J. Sprenz, W. Williams, K. Saunders, D. Montefiori, G. D. Sempowski, R. Henderson, M. Alam, B. F. Haynes, P. Acharya
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" conformations. Here, we report that the commonly used stabilized S ectodomain construct "2P" is sensitive to cold temperature, and that this cold sensitivity is resolved in a "down" state stabilized spike. Our results will impact structural, functional and vaccine studies that use the SARS-CoV-2 S ectodomain.
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