Cold sensitivity of the SARS-CoV-2 spike ectodomain

R. Edwards, K. Mansouri, V. Stalls, K. Manne, Brian E Watts, R. Parks, K. Janowska, S. Gobeil, Megan F. Kopp, Dapeng Li, X. Lu, Z. Mu, Margaret Deyton, T. Oguin, Jordan Sprenz, W. Williams, K. Saunders, D. Montefiori, G. Sempowski, R. Henderson, S. Munir Alam, B. Haynes, P. Acharya

Nature structural & molecular biology, 2021

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.

Cited by 9 publications.

Field of study: Medicine

10.1038/s41594-020-00547-5