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| Title | Cold sensitivity of the SARS-CoV-2 spike ectodomain. |
|---|---|
| Journal, issue, pages | bioRxiv, Year 2020 |
| Publish date | Oct 13, 2020 |
Authors | Robert J Edwards / Katayoun Mansouri / Victoria Stalls / Kartik Manne / Brian Watts / Rob Parks / Katarzyna Janowska / Sophie M C Gobeil / Megan Kopp / Dapeng Li / Xiaozhi Lu / Zekun Mu / Margaret Deyton / Thomas H Oguin / Jordan Sprenz / Wilton Williams / Kevin Saunders / David Montefiori / Gregory D Sempowski / Rory Henderson / Munir Alam / Barton F Haynes / Priyamvada Acharya |
| PubMed 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 ...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. |
External links | bioRxiv / PubMed:32699852 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 10.7 - 16.8 Å |
| Structure data | ![]() EMDB-22934: ![]() EMDB-22967: ![]() EMDB-22968: |
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