当前位置: X-MOL 学术bioRxiv. Biochem. › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
Cold sensitivity of the SARS-CoV-2 spike ectodomain.
bioRxiv - Biochemistry Pub Date : 2020-10-13 , DOI: 10.1101/2020.07.12.199588
Robert J Edwards , Katayoun Mansouri , Victoria Stalls , Kartik Manne , Brian Watts , Rob Parks , Katarzyna Janowska , Sophie M. C. Gobeil , Dapeng Li , Xiaozhi Lu , Margaret Deyton , Jordan Sprenz , Wilton Williams , Kevin Saunders , Gregory D. Sempowski , Rory Henderson , Munir Alam , Barton F. Haynes , Priyamvada Acharya

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.

中文翻译:

SARS-CoV-2 刺突胞外域的冷敏感性。

SARS-CoV-2 刺突 (S) 蛋白是 COVID-19 疫苗开发的主要目标,它的受体结合域具有两种构象:受体可接近的“向上”或受体不可接近的“向下”构象。在这里,我们报告了常用的稳定 S ectodomain 构造“2P”对低温敏感,并且这种冷敏感性在“向下”状态稳定尖峰中得到解决。我们的结果将影响使用 SARS-CoV-2 Sectodomain 的结构、功能和疫苗研究。
更新日期:2020-10-13
down
wechat
bug