Author: Edwards, Robert J; Mansouri, Katayoun; Stalls, Victoria; Manne, Kartik; Watts, Brian; Parks, Rob; Janowska, Katarzyna; Gobeil, Sophie M. C.; Kopp, Megan; Li, Dapeng; Lu, Xiaozhi; Mu, Zekun; Deyton, Margaret; Oguin, Thomas H; Sprenz, Jordan; Williams, Wilton; Saunders, Kevin O.; Montefiori, David; Sempowski, Gregory D.; Henderson, Rory; Alam, S. Munir; Haynes, Barton F.; Acharya, Priyamvada
Title: Cold sensitivity of the SARS-CoV-2 spike ectodomain Cord-id: e3wd75om Document date: 2021_1_5
ID: e3wd75om
Snippet: 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-
Document: 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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