Duke Human Vaccine Institute, Durham, NC, USA.
Department of Medicine, Duke University, Durham, NC, USA.
Nat Struct Mol Biol. 2021 Feb;28(2):128-131. doi: 10.1038/s41594-020-00547-5. Epub 2021 Jan 5.
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.
严重急性呼吸综合征冠状病毒 2 刺突（S）蛋白是 COVID-19 疫苗开发的主要靶点，其受体结合域呈现两种构象，即受体可及的“朝上”或受体不可及的“朝下”状态。在这里，我们报告说，常用的稳定 S 胞外域结构“2P”对低温敏感，而这种低温敏感性在稳定的“朝下”状态的胞外域中被消除。我们的发现将影响使用 SARS-CoV-2 S 胞外域的结构、功能和疫苗研究。
