Cold sensitivity of the SARS-CoV-2 spike ectodomain.
Journal Article (Journal Article)
The SARS-CoV-2 spike (S) protein, a primary target for COVID-19 vaccine development, presents its receptor binding domain in two conformations, the receptor-accessible 'up' or receptor-inaccessible 'down' states. Here we report that the commonly used stabilized S ectodomain construct '2P' is sensitive to cold temperatures, and this cold sensitivity is abrogated in a 'down' state-stabilized ectodomain. Our findings will impact structural, functional and vaccine studies that use the SARS-CoV-2 S ectodomain.
Full Text
Duke Authors
- Acharya, Priyamvada
- Gobeil, Sophie
- Henderson, Rory
- Montefiori, David Charles
- Saunders, Kevin O'Neil
- Sempowski, Gregory David
- Williams, Wilton Bryan
Cited Authors
- Edwards, RJ; Mansouri, K; Stalls, V; Manne, K; Watts, B; Parks, R; Janowska, K; Gobeil, SMC; Kopp, M; Li, D; Lu, X; Mu, Z; Deyton, M; Oguin, TH; Sprenz, J; Williams, W; Saunders, KO; Montefiori, D; Sempowski, GD; Henderson, R; Munir Alam, S; Haynes, BF; Acharya, P
Published Date
- February 2021
Published In
Volume / Issue
- 28 / 2
Start / End Page
- 128 - 131
PubMed ID
- 33402708
Pubmed Central ID
- PMC7878407
Electronic International Standard Serial Number (EISSN)
- 1545-9985
Digital Object Identifier (DOI)
- 10.1038/s41594-020-00547-5
Language
- eng
Conference Location
- United States